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Early Career Investigator Recognition

December 2010

 

Manjunatha M. Venkataswamy, Ph.D.

Albert Einstein College of Medicine, US
Nominated by Dr. Norman Letvin

Dr. Manjunatha M. Venkataswamy received his Ph.D in Microbiology in 2005 from the National Institute of Mental Health and Neurosciences in India, where his research was focused on tuberculous meningitis (TBM). His graduate research there involved genotyping of clinical isolates of M. tuberculosis from patients with TBM and evaluation of rapid diagnostic methods for this form of tuberculosis (TB).

Following his graduate studies he joined the laboratory of Dr. Steven Porcelli at the Albert Einstein College of Medicine as a postdoctoral fellow. The principal area of his postdoctoral research has been in the evaluation of adjuvant activity of the Natural Killer T (NKT) cell activating glycolipid alpha-galactosylceramide and its synthetic analogues with the live attenuated vaccine M.bovis BCG in the mouse model. This research led to the development of a novel method for incorporating these glycolipid adjuvants into live BCG, resulting in a vaccine with enhanced immunogenicity and protective efficacy against TB. Currently his efforts are focused on evaluating adjuvant activity of novel glycolipid analogues and alternate methods for optimal incorporation of adjuvants into live attenuated mycobacterial vaccines.

He is currently an Associate at the Albert Einstein College of Medicine. Being a member of the Letvin rMycobacteria VDC since 2008, his role has been to use the adjuvant incorporation approach to enhance the immunogenicity against a BCG vectored SIV vaccine. This has resulted in a vaccine which shows enhanced priming of CD8 T cells in mice to the SIV-Gag antigen.

November 2010

 

Ron Diskin, Ph.D.

California Institute of Technology, US
Nominated by Dr. Leo Stamatatos

Dr. Ron Diskin is a member of the Stamatatos VDC and a postdoctoral research scientist at the California institute of Technology working in the laboratory of Dr. Pamela Bjorkman. He received his Bachelor’s degree in Life Sciences from the Hebrew University of Jerusalem. Subsequently, he began his graduate research on developing and characterizing active forms of mitogen-activated protein kinases using X-ray crystallography and biochemistry methods in the lab of Dr. Oded Livnah at the Hebrew University of Jerusalem, where he obtained his Master’s Degree followed by his Ph.D. in 2007.

Dr. Diskin’s current research is focused on revealing the structural diversity of the spike proteins from different HIV clades to facilitate better vaccine design and to understand the structural mechanisms underlying resistance to neutralizing antibodies. Recently, Diskin and colleagues provided the first crystal structure of a clade C gp120 in complex with 21c CD4i-Ab and CD4 (Diskin, et al. 2010, Nature Structural & Molecular Biology). Solving this crystal structure allowed a first-time comparison between a clade B and a clade C gp120 structures. Additionally, the crystal structure uncovered that 21c is an auto-reactive antibody that recognizes an epitope which spans both the viral gp120 protein and the human CD4 receptor.

Currently, Dr. Diskin is continuing his efforts to provide additional structural information of the spike complex and its individual protein components from a diversity of different HIV strains.

October 2010

 

Florencia Pereyra, MD

Ragon Institute of MGH, MIT, and Harvard, US
Nominated by Dr. Bruce Walker

Dr. Florencia Pereyra is a physician scientist at the Ragon Institute of MGH, MIT, and Harvard and the Division of Infectious Diseases at Brigham and Women's Hospital. She completed her medical training at the Universidad Central de Venezuela, her Internal Medicine training at Albert Einstein Medical Center and her Infectious Diseases training at Massachusetts General Hospital and Brigham and Women’s Hospital combined fellowship program. She joined the laboratory of Bruce Walker during her postdoctoral research training.

Dr. Pereyra’s research interest is in host genetic and immunologic correlates of HIV control. Within the Walker Vaccine Discovery Consortium she led the establishment of what is now the largest existing cohort and biological sample repository of spontaneous HIV controllers in the world (The International HIV Controllers Study). This cohort of well pedigreed individuals is being used by the group to identify innate and adaptive immune, viral and host genetic correlates of HIV control and their implications for immunogen design.

She has worked for the past 4 years in a genome wide association study that included 1000 HIV controllers and 2500 chronic progressors, in this study substantial progress was made in identifying new genetic variants and explaining the classical HLA associations with durable control of HIV. In addition her work in assessing the differential contribution of T cell responses in HIV controllers has resulted in the identification of epitope specific CD8+ T cell responses that are associated with spontaneous viral control and can be used to inform immunogen design.

Maxim Totrov, PhD

Molsoft LLC, US
Nominated by Dr. Susan Zolla-Pazner

Dr. Maxim Totrov is a member of the Zolla-Pazner Vaccine Discovery Consortium and the Principal Scientist at Molsoft, a small biotechnology company based in La Jolla, CA. He completed his PhD studies in biophysics at the lab of Dr Abagyan at NYU in 1999. His graduate work resulted in novel algorithms for macromolecular docking and energy calculations. Following postdoctoral studies at the Scripps Research Institute, Dr. Totrov joined Molsoft in 2000.

Dr. Totrov’s research is focused on the development and application of in-silico methods for molecular design. In the vaccine design field, he is particularly interested in optimal presentation of immunogenic epitopes on scaffold proteins. Appropriate choice of scaffold and placement of the epitope within its tertiary structure should result in a stable construct and constrain the epitope to the desired conformation or a range of conformations. In a recently published study (Totrov et al. Virology 2010 405(2):513-23) two such constructs based on CTB were designed, expressed and evaluated immunologically. Immunogen presenting complete V3 loop from HIV gp120 on the CTB scaffold induced high titers of neutralizing antibodies in rabbit sera. Several follow-up designs are currently undergoing evaluation. In another development, a ‘mimotope’ constrained peptide was designed to present a conformation of the V3 that is recognized by a particular large class of neutralizing anti-V3 Abs (Jiang et al 2010 Nature Struct & Mol Biol 17(8):955-61). This peptide can now be grafted on another scaffold to specifically elicit antibodies of this particular class.

September 2010

 

Zhen-Yu Jim Sun, PhD

Harvard Medical School, US
Nominated by Dr. Ellis Reinherz & Dr. Gerhard Wagner

Dr. Zhen-Yu J. Sun received his Ph.D. in physics at Carnegie Mellon University, Pittsburgh, PA. He received postdoctoral research training in the laboratory of Gerhard Wagner and is currently a Research Associate at Harvard Medical School. One of his major research interests is in the use of nuclear magnetic resonance (NMR) spectroscopy as a structural tool to analyze the HIV envelop protein for vaccine design.

Although rarely elicited during natural human infection, the most broadly neutralizing antibodies (BNAbs) against diverse HIV-1 strains target the membrane-proximal ectodomain region (MPER) of viral gp41. To gain insight into MPER antigenicity, immunogenicity, and viral function, he studied its structure in the lipid environment by NMR and discovered its characteristic helix-hinge-helix motif. Combining with data from electron paramagnetic resonance (EPR), and surface plasmon resonance (SPR) techniques, the analyses revealed this metastable L-shaped structure is immersed in viral membrane and, therefore, less accessible to immune attack. Nonetheless, more data suggested that 4E10 BNAb extracts buried W672 and F673 after initial encounter with the surface-embedded MPER and, given conservation of MPER sequences in HIV-1, HIV-2, and SIV, have important implications for structure-guided vaccine design.

Within the Reinherz VDC, Dr. Sun continues to analyze MPER segments of clade C virus in an effort to understand how variation in sequences might effect the conformation of the MPER in the membrane environment. He is additionally investigating the structure of the MPER in various membrane mimics and those conformations relative to its interaction with BNAbs.

August 2010

 

Joshua Klein, PhD

California Institute of Technology, US
Nominated by Dr. Leo Stamatatos

Dr. Joshua Klein is a member of the Stamatatos VDC and a postdoctoral research scientist at the California Institute of Technology working jointly in the laboratories of Dr. Pamela Bjorkman and Dr. David Baltimore. Following the completion of his Bachelor’s degree at UC Berkeley while a researcher in the trace gas biogeochemistry laboratory of Dr. Allen Goldstein, Dr. Klein joined the Bjorkman laboratory, where he obtained his Ph.D. in 2009.

Dr. Klein’s research is focused on characterizing the relationship between antigen density and antibody avidity in the neutralization of HIV. Their biochemical investigations and structural modeling using available X-ray crystallography and electron cryomicroscopy data suggest that bivalent binding is rare for many of the broadly neutralizing antibodies, whether by binding to epitopes between spikes or within a spike trimer (Klein, et al. 2009, PNAS; Klein and Bjorkman, 2010, PLoS Pathogens). To overcome this limitation, they are working on the development of novel antibody architectures to enhance antibody avidity to HIV using human-derived small protein fusions that force extended conformations between the Fabs of an IgG. These redesigned antibodies may be useful as passive immunotherapies and/or gene therapies to treat and prevent HIV infection with greater potency than the naturally occurring structures of IgG antibodies.

David Lutje Hulsik, PhD

Unit of Virus Host Cell Interactions, FR
Nominated by Dr. Robin Weiss

Dr. David Lutje Hulsik is currently a postdoctoral fellow in Professor Winfried Weissenhorn’s lab at the Unit of Virus Host Cell Interactions (UVHCI) in Grenoble. He completed his Ph.D. early 2009 in the lab of Professor Theo Verrips, Utrecht University, were he studied the intrinsic properties of broadly neutralizing llama heavy chain antibodies (VHHs) specific for the HIV-1 gp120 CD4 binding site.

Together with Dr. Andreas Hinz, a former member of the Weissenhorn lab, Dr. Lutje Hulsik has obtained a high resolution crystallographic structure of a single-chain, neutralizing antibody fragment (VHH) derived from llamas immunized with subtype C HIV-1 gp120. Mutational analysis identified CDR3 as a key component of gp120 interaction as determined by surface plasmon resonance. A decrease in affinity is directly coupled to the neutralization efficiency since mutations that decrease gp120 interaction increase the IC50 required for HIV-1 IIIB neutralization. Thus the structural study identifies the long CDR3 of D7 as the key determinant of interaction and HIV-1 neutralization. This research was conducted in collaboration with the groups of Theo Verrips and Robin Weiss at UCL and has been published in PLoS One (2010 May 5;5(5):e10482).

Currently Dr. Lutje Hulsik studies the structure(s) of MPER-specific VHH with neutralizing activities, which have been isolated from gp41-immunized llamas. He is also continuing to improve the design of MPER antigens in order to increase their immunogenicity and capability to induce neutralizing antibodies.

July 2010

 

Munir Alam, PhD

Duke University, US
Nominated by Dr. Bart Haynes

Dr. Munir Alam is trained in Molecular Immunology and received his PhD from the University of Glasgow, U.K. He was a Commonwealth Association Scholar in UK and his graduate studies involved characterization of immunological and molecular markers associated with metastatic human breast cancer.

Following his graduate studies, he trained as a post-doctoral fellow with Dr. Nick Gascoigne in the Department of Immunology at Scripps Research Institute. At Scripps, Dr. Alam’s work resulted in significant contributions in the field of T cell recognition and development. One of his most influential works involves the measurement of soluble TCR and MHC-peptide binding affinity and the correlation between TCR avidity and thymic selection. His subsequent studies contributed to further our understanding of how T cells distinguish between strong or weak agonist ligands during T cell activation. He also studied the role of TCR V allelic exclusion during selection and maturation of thymic T cells.

Dr. Alam joined the Duke Human Vaccine Institute in 2000, and he is currently an Associate Professor in Medicine. The Alam laboratory's basic research is targeted at developing new ways to monitor and enhance vaccine responses against HIV-1. Dr. Alam’s lab is particularly interested in understanding the basis of polyspecificity of broadly neutralizing HIV-1 antibodies and the relevance of antibody membrane lipid binding in HIV-1 neutralization. His work within the Haynes CAVD has led to the design of several gp41 immunogens that present the neutralizing epitopes in the context of membrane. Their recent work suggests that viral membrane lipid binding may be a required initial step for HIV-1 neutralization by gp41neutralizing antibodies. Using Toll like receptor agonists, they have also designed adjuvants conjugated to liposomal particles which are now being used as immmunogen-adjuvant complexes for the induction of HIV-1 neutralizing antibodies.

 

Willie Koh, PhD

University College London, UK
Nominated by Dr. Robin Weiss

Dr. Willie Koh is currently a postdoctoral researcher in Professor Robin Weiss's lab at University College London (UCL), having just recently completed his Ph.D. in the same lab. Prior to this, Dr. Koh received his Bacelor's and Master's degrees at the National University of Singapore, and has worked on host-virus interactions of flaviviruses.

Over the past 5 years, Dr. Koh has investigated the use of small single-chain antibody fragments (VHH) as potential inhibitors of HIV-1 infection. These VHH are derived from llamas immunized with HIV-1 gp120 of subtype C and have potential uses as microbicides and in vaccine design. By taking a prototype fairly broadly neutralizing VHH that binds to an epitope on gp120 near the CD4 binding site, Dr. Koh exploited degenerate reverse PCR primers located at the N-terminus of the CDR3 region of the antibody to amplify the complete set of affinity maturation variants of this VHH family in the phage library. All the variants had neutralizing properties but some with a particular sequence in the CDR3 region were more potent and more broadly neutralizing than others. This technique represents a powerful new method to select and design a family-specific set of HIV-1 neutralizing monoclonal antibodies. This research was conducted in collaboration with the group of Theo Verrips at the University of Utrecht as part of the UCL VDC and has recently been published (Koh et al., J Biol Chem 2010 285:19116).

June 2010

 

Hengyu (Carina) Xu, PhD

Fred Hutchinson Cancer Research Center, US
Nominated by Dr. Leo Stamatatos & Dr. Roland Strong

Dr. Xu is a postdoc fellow at Fred Hutchinson Cancer Research Center, trained by Dr. Roland Strong. Her research is focused on understanding how 4E10 broadly neutralizes HIV isolates, and how to elicit 4E10-like response through immunization. 4E10 is known to bind to its linear epitope as well as viral membrane. However, her group has found that the 4E10-membrane binding is extremely weak. They were able to generate a mutant that reduces 4E10-membrane binding without affecting its neutralization. They also characterized binding of 4E10 to monomeric, trimeric gp140s comparing to its binding to linear epitope. Affinities to gp140s were 10-fold weaker than to epitope, suggesting that in the context of gp140, the 4E10 epitope is constrained to adopt a conformation significantly different from the ideal binding conformation. In order to visualize the binding of 4E10 to gp140 trimer, they have generated SAXS model of 4E10-gp140trimer complex, which clearly shows a huge conformational change on gp140 trimer upon 4E10 binding. To elicit 4E10-like response, they have biophysically characterized hundreds of computationally designed non-HIV protein scaffolds presenting conserved 4E10 epitope, developed protocol to rapid examine serum responses against designed scaffolds using SPR.

Dr. Xu received her PhD in Chemistry and Biochemistry at the University of Oklahoma in 2007. Her graduate work contributed significantly to the field's understanding of the kinetic & chemical mechanisms, substrate specificities, structure and function of saccharopine dehydrogenase, one of the key enzymes in the lysine biosynthesis pathway in fungi.

May 2010

 

Mikyung Kim, PhD

Dana-Farber Cancer Institute, US
Nominated by Dr. Ellis Reinherz

Dr. Mikyung Kim received her Ph.D. in Biochemisty from Chonbuk National University in Korea, where she studied the enzymatic process of production of oligo-fructose from inulin. She has worked as a post-doctoral fellow and then instructor at Harvard Medical School and DFCI within the Laboratory of Immunobiology on the structure-based immunogen design to elicit broadly neutralizing antibody (BNAb) against HIV.

Within the Reinherz VDC, Dr. Kim's work focuses on understanding how BNAbs that recognize the membrane proximal external region (MPER) of HIV-1 gp41 bind to their lipid-embedded epitopes and mediate anti-viral activity. Dr. Kim and her colleagues in the Reinherz VDC of the CAVD, using EPR and NMR methods, have recently shown that BNAbs disrupt HIV-1 MPER fusogenic functions critical for viral entry into human cells by two distinct modes: 2F5 and 4E10 perturb MPER orientation by inducing large conformational changes in the MPER relative to the membrane. Z13e1 prevents hinge motion, immobilizing the MPER hinge through extensive rigidifying surface contacts. The lipid interaction with 4E10 has further proved to be important for the extraction of its core epitope. Dr. Kim is currently employing immunogens based upon these insights for delivery of lipid particles displaying the MPER to elicit such protective antibodies.

Thomas Matt Holl

Duke University, US
Nominated by Dr. Bart Haynes

Mr. Thomas Matt Holl is a graduate student of Garnett Kelsoe D.Sc. in the Department of Immunology at Duke University. Mr. Holl has investigated whether some classes of broadly neutralizing HIV-1 antibodies are purged from the B-cell repertoire during development. Working with CAVD investigator, Laurent Verkoczy, Mr. Holl demonstrated that the 2F5 BNAb reacted with both human- and mouse self-antigens, thereby validating the use of knock-in mouse strains to elucidate the impact of B-cell tolerance on HIV-1 antibody responses.

Independently, Mr. Holl has demonstrated the loss of potential BNAb precursors coincident with a known check-point of B cell tolerance, a finding consistent with the tolerization of certain HIV-reactive B cell populations in normal mice. This observation led Mr. Holl to develop and characterize a novel culture system that supports B-cell development and maturation absent the tolerizing environment of the bone marrow. These culture-derived (CD) B cells are significantly enriched for auto-reactive and HIV-1 MPER-reactive clones. These “forbidden” B cells are stably maintained in lymphocyte deficient, congenic hosts where they produce high levels of serum IgM and IgG autoantibody. CD cell reconstituted mice respond significantly better to MPER peptide antigens than control animals and he is currently using them to compare the efficacy of HIV-1 MPER vaccine constructs.

Mr. Holl completed his undergraduate degree in Microbiology at the University of Pittsburgh in 1999. Before arriving at Duke University, Mr. Holl worked at The Jackson Laboratory in Bar Harbor, Maine where he investigated the role of MHC haplotype restriction of cytotoxic CD8+ T cells in Type1 diabetes.

April 2010

 

Elin Gray, PhD

National Institute for Communicable Diseases, South Africa
Nominated by Dr. David Montefiori

Dr. Elin Gray works within Dr. David Montefiori’s Vaccine Immune Monitoring Consortium. She is part of the R&D team working on the development of assays that can be used to map the epitopes on the envelope glycoprotein of HIV-1 recognized by broadly cross-neutralizing antibodies found in plasma of some infected individuals.

Dr. Gray received her PhD in Medicine 2008 from the University of the Witwatersrand, Johannesburg, South Africa in 2008. She studied the neutralization epitopes on HIV-1 subtype C envelope glycoproteins, under the mentorship of Prof. Lynn Morris. She also participated in HIV clinical vaccine trials in South Africa and the standardization of various immunoassays.

After obtaining her PhD, Dr. Gray continued working in the Morris’ lab at the National Institute for Communicable Diseases (NICD) as a post-doctoral fellow. In particular she has been researching the development of broadly neutralizing antibodies during natural infection, the epitopes recognized by these antibodies and the factors associated with this response. Dr. Gray is also interested in the relationship between ongoing viral escape from autologous neutralizing antibodies and the emergence of neutralization breadth.

March 2010

 

George Sellhorn, PhD

Seattle Biomedical Research Institute, US
Nominated by Dr. Leo Stamatatos

Dr. George Sellhorn is a member of the Stamatatos VDC and a postdoctoral research scientist at Seattle Biomedical Research Institute. Dr. Sellhorn obtained his Ph.D. from the Graduate Program in Molecular Plant Sciences at Washington State University in 2006 following the completion of his B.Sc. in biology from Indiana University in 1999. His graduate studies investigated the structure and function of soybean vegetative lipoxygenases.

Dr. Sellhorn joined the Stamatatos lab in June of 2006 to lead the immunogen expression and purification efforts. Dr. Sellhorn has worked for the past three and a half years establishing a high throughput platform for mammalian expression of diverse soluble HIV-1 Envelop proteins and developed an efficient Envelope production and purification protocol which routinely produces milligram quantities of Envelope trimers. His efforts provide material for Envelope-immunization studies in addition to supplying protein for Envelope crystallization. More recently, Dr. Sellhorn was successful in engineering, expressing and purifying stable, soluble heterotrimeric Envelope proteins which are composed of both clade A and clade B protomers. These novel constructs are currently being tested as immunogens in animals.

Davide Corti, PhD

Institute for Research in Biomedicine, Switzerland
Nominated by Prof. Robin Weiss

Dr. Davide Corti is currently Director of the Antibody Discovery Unit at Humabs LLC, a spin-out company of the Institute of Research in Biomedicine. Dr. Corti completed his Ph.D. in Antonio Lanzavecchia’s laboratory in December 2007 where he studied the human memory B cell repertoire as an accessible source of all the antibody specificities produced during the lifespan of an individual. The dissection of the memory B cell repertoire was performed using two independent approaches: the first aimed to establish frequency and fine specificity of memory B cells for a variety of human pathogens and their kinetics following infection or vaccination, the second aimed to interrogate the B cell repertoire for the isolation of human monoclonal antibodies (mAbs) that would be capable of broadly neutralize viral targets, such as SARS-CoV, Influenza A and HIV-1. The isolation of broadly neutralizing monoclonal antibodies is relevant not only for serotherapy, but also for “analytic vaccinology” where such antibodies are used as probes to identify conserved epitopes that may be properly formulated as vaccines. Dr. Corti’s work in the Weiss CAVD consortium has centered on the isolation of novel monoclonal antibodies that neutralize many strains of HIV-1 from selected patients of the Antwerp and London’s cohorts. Three particularly interesting mAbs (HJ16, HGN194 and HK20) have been mapped to the CD4 binding site, the V3 loop and gp41 HR1, respectively, and characterized within the Weiss-VDC and by the Duke University VIMC. The initial results have recently been published (Corti D et al, 2010, PLoS One).

February 2010

 

Erica Andersen-Nissen, PhD

Fred Hutchinson Cancer Research Center, US
Nominated by Dr. Julie McElrath

Dr. Erica Andersen-Nissen is currently a postdoctoral research fellow in the laboratory of Dr. Julie McElrath at the Fred Hutchinson Cancer Research Center. Erica completed her Ph.D. at the University of Washington in June 2006 where she studied the role of Toll-like receptor 5 (TLR5) in the innate immune response to bacterial flagellin, under the mentorship of Dr. Alan Aderem. Her work contributed significantly to the field’s understanding of TLR-agonist interactions and highlighted the significance of TLR5 to the innate immune response in vivo.

Erica’s work in the McElrath CAVD consortium has centered on understanding the innate immune responses induced by candidate HIV vaccines. She profiled immune responses within one week following immunization with the MRKAd5 HIV vaccine. After vaccination, she observed rapid alterations in blood leukocyte populations, induction of cytokines, and dramatic transcriptional changes in PBMC. Comparing MRKAd5 to yellow fever vaccine (YFV) revealed that although the MRKAd5 response was more rapid and transient, the genes affected by MRKAd5 and YFV overlap significantly. Finally, pre-existing Ad5 neutralizing antibodies resulted in greatly attenuated responses to MRKAd5. These results provide the first systems view of human innate immune responses to a candidate HIV vaccine. Erica’s work forms an integral part of our CAVD consortium and she has incorporated the innate immune studies into various HIV vaccine candidate regimens. These studies will provide new information about responses in humans to experimental adjuvants and other viral vector platforms.

Weizao Chen, PhD

National Cancer Institute, National Institutes of Health, US
Nominated by Dr. Bart Haynes

Dr. Weizao Chen obtained his PhD in Microbiology from Fudan University in China in 2006, where he developed subunit vaccines against foot-and-mouth disease viruses (FMDV) and evaluated RNA interference as a novel FMDV therapeutics. He joined Dr. Dimiter S. Dimitrov’s group at the National Cancer Institute (NCI), National Institute of Health (NIH) as a postdoctoral fellow in 2006.

During postdoctoral training, Dr. Chen constructed human antibody libraries from healthy and HIV-1 infected individuals for selection of HIV-specific monoclonal antibodies with implications for HIV-1 vaccine design. He developed the first reported human domain antibody (dAb) against HIV-1, m36, which was selected from a large human dAb library and highly efficiently neutralized HIV-1 isolates from different clades. M36 is very small (size, ~15 kDa), targets a highly conserved sterically restricted structure on gp120 and therefore, could also be used as a valuable reagent for probing the hidden neutralizing determinants of HIV-1 envelope glycoproteins. Recently, Dr. Chen selected several high-affinity antibodies which target highly conserved structures on gp120 and gp41 while do not neutralize or enhance infection by primary isolates suggesting the existence of antigenic conserved structures that could direct the immune response to non-neutralizing or even enhancing antibodies which may represent a strategy used by the virus to escape neutralizing immune responses. Dr. Chen sequenced and is analyzing an antibody repertoire from an HIV-1 patient whose serum exhibits 2F5-like neutralizing activity which could provide knowledge for basic understanding of immune responses to HIV-1 and help in the design of effective vaccine immunogens.

January 2010

 

Yongjun Guan, PhD

Institute of Human Virology, University of Maryland, US
Nominated by Dr. Robert Gallo

Dr. Yongjun Guan received his Ph.D. in Immunology from China CDC in 1998. He then continued training in Molecular Virology and Viral Immunology as post-doctoral fellow at McGill University (Dr. Mark Wainberg’s lab) and University of Toronto (Dr. Kelly MacDonald’s Lab). He joined the Institute of Human Virology in 2004 and was appointed as Assistant Professor in 2009.

Dr. Guan started his research works on AIDS vaccine development in 1994. His Ph. D. works were on AIDS vaccine candidates of virus-like particles and DNA/rAAV vaccine. During post-doctoral training, Dr. Guan designed and constructed a hyper-attenuated SIV as AIDS vaccine model, which showed protection in monkey trial. He also evaluated the AIDS vaccine strategy of allo-MHC immunization in monkey model and showed that allo-MHC immunization alone is not protective. After joining the IHV, Dr. Guan demonstrated that human CD4 T cells can self-defend against R5 HIV-1 by secreting anti-viral chemokines and pointed out that AIDS vaccine candidate should selectively elicit CD4 T cell responses capable of ‘‘self-protection’’.

Dr. Guan’s works within the Gallo VDC is focused on the identification of functional Ab response against Env in HIV controller and monkey model. His work demonstrated discordance between Env specific memory B cells and serologic anti-Env antibodies and indicated the importance of memory B cell pool as a historical reservoir of humoral immune responses. Most important, he developed a novel practical method for rapid cloning of mAb from memory B cell to identify functional mAbs from HIV-1 controller and monkey model.

Alexandre Harari, PhD

Vaccine and Immunotherapy Center, CHUV, Switzerland
Nominated by Dr. Richard Koup

Dr. Alexandre Harari received his PhD degree from the University Of Lausanne, Switzerland in 2002 and is currently project leader at the Vaccine and Immunotherapy Center directed by Dr. Giuseppe Pantaleo. Over the past decade, Dr. Harari’s research interests were antiviral cellular immunity and vaccine-induced T-cell responses.

Recently, Dr. Harari has investigated the mechanism of cytotoxic activity of antigen-specific CD8 T-cells. Cytotoxic CD8 T-cells mediate a fundamental protective role against virus infections and the induction of vigorous CD8 T-cell responses following vaccination is thought to be a key component of protective immunity. For these reasons, several studies have centered on the functional characterization of CD8 T-cells with the objective of identifying functional profiles that may correlate with protective CD8 T-cell responses. Dr. Harari’s studies showed that distinct profiles of cytotoxic granules can be identified in different virus-specific memory CD8 T-cells and that there is a hierarchy among the cytotoxic granules in setting the efficiency of cytotoxic activity with Perforin being the most powerful correlate of cytotoxic function, followed by GrmB.

 

 

2016 Early Career Investigators

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2015 Early Career Investigators

To view the honorees that occured in 2015, click the following link: 2015 Early Career Investigators

2014 Early Career Investigators

To view the honorees that occured in 2014, click the following link: 2014 Early Career Investigators

2013 Early Career Investigators

To view the honorees that occured in 2013, click the following link: 2013 Early Career Investigators

2012 Early Career Investigators

To view the honorees that occured in 2012, click the following link: 2012 Early Career Investigators

2011 Early Career Investigators

To view the honorees that occured in 2011, click the following link: 2011 Early Career Investigators

2010 Early Career Investigators

To view the honorees that occured in 2010, click the following link: 2010 Early Career Investigators

2009 Early Career Investigators

To view the honorees that occured in 2009, click the following link: 2009 Early Career Investigators

 
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