Virology
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XINZHEN YANG,  M.D.,Ph.D.

Assistant Professor in Medicine

Division of Viral Pathogenesis Telephone: Tel:  (617)667-2052
Beth Israel Deaconess Medical Center      Fax: (617)667-8210
330 Brookline Avenue                             Email:  xyang1@bidmc.harvard.edu
E/CLS-1011
Boston, MA 02215


RESEARCH INTERESTS:

The main interests of this laboratory are in basic virological and immunological aspects of HIV-1 envelope glycoproteins.   HIV-1 carries very few envelope glycoprotein units or spikes, a unique phenomenon among enveloped viruses.  We are investigating the basis of it as well as its functional consequences in virus entry, immunogenicity and antigenecity.  As a lentivirus that needs to survive in the host for a long period of time in clinical latency, HIV-1 infection induces very low level of neutralizing antibody responses only sporadically.  We are interested in characterizing the rare cases in which broad and potent neutralizing antibodies against HIV-1 are induced, in terms of what neutralizing epitopes on HIV-1 envelope glycoproteins are targeted and how HIV-1 can cope with the presence of such strong neutralizing antibodies in vitro and in vivo.  Developing an effective prophylactic vaccine against HIV-1 infection is still of the highest priority in the field of HIV-1 and AIDS research. Our research interests in HIV-1 vaccinology are in the broadest terms.  We investigate the theoretical framework on the fundamental mechanisms of antibody-mediated neutralization of HIV-1 as well as other enveloped viruses in general.  Finally, we develop novel immunogens and vaccine formulations based on HIV-1 glycoproteins aimed at inducing broad and potent neutralizing antibody responses to HIV-1.

 

 

Yang X, Wyatt R and Sodroski J. Trimer formation by soluble HIV-1 envelope glycoproteins enhances its immunogenicity to elicit neutralizing antibodies. J Virol 2000;75:1165-71.

Ren X, Sodroski J, and Yang X. An Unrelated Monoclonal Antibody Neutralizes Human Immunodeficiency Virus (HIV-1) by Binding to an Artificial Epitope Engineered in a Functionally Neutral Region of the Viral Envelope Glycoproteins. J. Virol. 2005; 79:5616-5624.

Yang X, et al. Distinct Entry Stoichiometry of Human Immunodeficiency Virus, Murine Leukemia Virus and Influenza Virus. J. Virol. 2005; 79: 12132-12147.

Yang X, et al. Antibody binding is a dominant determinant of the efficiency of human immunodeficiency virus type 1 neutralization. J Virol. 2006; 80:11404-11408.

Zhou T, et al. Structural definition of a conserved neutralization epitope on HIV-1 gp120. Nature, 2007; 445:732-737.

Yang X, et al. Antibody Binding in Proximity to the Receptor/Glycoprotein Complex Leads to a Basal Level of Virus Neutralization. J. Virol. 2007; 81:8809-8813