Mei Yun Zhang
Affiliation: National Cancer Institute
- Selection of a novel gp41-specific HIV-1 neutralizing human antibody by competitive antigen panningMei Yun Zhang
Protein Interactions Group, CCRNP, CCR, NCI Frederick, NIH, Frederick, Maryland 21702, USA
J Immunol Methods 317:21-30. 2006..These results may have implications for the selection of novel gp41-specific bcnAbs and other antibodies, and for the development of HIV-1 inhibitors and vaccine immunogens...
- Novel approaches for identification of broadly cross-reactive HIV-1 neutralizing human monoclonal antibodies and improvement of their potencyMei Yun Zhang
Protein Interactions Group, CCRNP, CCR, NCI Frederick, NIH, Bldg 469, Rm 131, P O Box B, Miller Drive, Frederick, MD 21702 1201, USA
Curr Pharm Des 13:203-12. 2007..The further characterization of the molecular interactions of the bcnAbs with gp120-gp41 will undoubtedly help in our understanding of the mechanisms of virus neutralization, and in the design of entry inhibitors and vaccines...
- Cross-reactive human immunodeficiency virus type 1-neutralizing human monoclonal antibody that recognizes a novel conformational epitope on gp41 and lacks reactivity against self-antigensMei Yun Zhang
CCRNP, CCR, NCI Frederick, NIH, Bldg 469, Rm 131, P O Box B, Miller Drive, Frederick, MD 21702 1201, USA
J Virol 82:6869-79. 2008..Its novel conserved conformational epitope on gp41 could be helpful in the design of vaccine immunogens and as a target for therapeutics...
- Sequential antigen panning for selection of broadly cross-reactive HIV-1-neutralizing human monoclonal antibodiesMei Yun Zhang
SAIC Frederick, Inc, NCI Frederick, Frederick, MD 21702, USA
Methods Mol Biol 562:143-54. 2009..This methodology could be used to isolated recombinant antibodies against any antigen that shares epitopes with other antigens...
- Identification and characterization of a new cross-reactive human immunodeficiency virus type 1-neutralizing human monoclonal antibodyMei Yun Zhang
Human Immunovirology Group, Laboratory of Experimental and Computational Biology, Center for Cancer Research, National Cancer Institute Frederick, NIH, Frederick, Maryland 21702 1201, USA
J Virol 78:9233-42. 2004....
- Identification of a novel CD4i human monoclonal antibody Fab that neutralizes HIV-1 primary isolates from different cladesMei Yun Zhang
Human Immunovirology and Computational Biology Group, LECB, CCR, NCI Frederick, NIH, Frederick, MD 21702, USA
Antiviral Res 61:161-4. 2004..The identification of a new hmAb with broad neutralizing activity that exhibits differential inhibitory profile suggests a potential for its use as a component of anti-HIV-1 treatments...
- Broadly cross-reactive HIV neutralizing human monoclonal antibody Fab selected by sequential antigen panning of a phage display libraryMei Yun Zhang
Laboratory of Experimental and Computational Biology, CCR, NCI Frederick, NIH, Bldg 469, Rm 246, P O Box B, Miller Drive, Frederick, MD 21702 1201, USA
J Immunol Methods 283:17-25. 2003..The methodology and the results may have implications for development of HIV vaccines and inhibitors, as well as for identification of antibodies to conserved epitopes on rapidly mutating viruses and cells...
- Cross-reactive HIV-1 neutralizing monoclonal antibodies selected by screening of an immune human phage library against an envelope glycoprotein (gp140) isolated from a patient (R2) with broadly HIV-1 neutralizing antibodiesVidita Choudhry
Protein Interactions Group, CCRNP, NCI Frederick, NIH, Frederick, MD 21702, USA
Virology 363:79-90. 2007....
- Antibody-based inhibitors of HIV infectionVidita Choudhry
NCI Frederick, Protein Interactions Group, CCRNP, CCR, NIH, P O Box B, Frederick, MD 21702 1201, USA
Expert Opin Biol Ther 6:523-31. 2006..The challenge is whether an antibody-based therapy can be identified (with or without their small molecule brethren) that presents long-term clinical efficacy, low toxicity and minimal risk of clinical failure from viral resistance...
- Structural mimicry of CD4 by a cross-reactive HIV-1 neutralizing antibody with CDR-H2 and H3 containing unique motifsPonraj Prabakaran
Protein Interactions Group, Center for Cancer Research Nanobiology Program, National Cancer Institute, NIH, Frederick, MD 21702, USA
J Mol Biol 357:82-99. 2006..Thus, vaccine immunogens based on the m18 epitope structure are unlikely to elicit antibodies that could enhance infection. The structure can also serve as a basis for the design of novel, highly efficient inhibitors of HIV entry...
- Competitive antigen panning for selection of HIV-1 neutralizing human monoclonal antibodies specific for gp41Mei Yun Zhang
NCI Frederick, National Institutes of Health, Frederick, MD, USA
Methods Mol Biol 525:175-86, xv. 2009..It is superior to a traditional pre-depletion method in avoiding potential loss of target-specific antibodies...
- Increased efficacy of HIV-1 neutralization by antibodies at low CCR5 surface concentrationVidita Choudhry
Protein Interactions Group, CCRNP, CCR, NCI Frederick, NIH, Frederick, MD 21702, USA
Biochem Biophys Res Commun 348:1107-15. 2006....
- Germline-like predecessors of broadly neutralizing antibodies lack measurable binding to HIV-1 envelope glycoproteins: implications for evasion of immune responses and design of vaccine immunogensXiaodong Xiao
Protein Interactions Group, CCRNP, NCI Frederick, NIH, Frederick, MD 21702, USA
Biochem Biophys Res Commun 390:404-9. 2009..This hypothesis, if further supported by data, could contribute to our understanding of how HIV-1 evades immune responses and offer new concepts for design of effective vaccine immunogens...
- Cross-reactive HIV-1-neutralizing activity of serum IgG from a rabbit immunized with gp41 fused to IgG1 Fc: possible role of the prolonged half-life of the immunogenMei Yun Zhang
Center for Cancer Research Nanobiology Program, CCR, NCI Frederick, NIH, Frederick, MD 21702, USA
Vaccine 27:857-63. 2009..Further research is needed to confirm and extend these results which may have implications for the development of vaccine immunogens with enhanced capability to elicit cross-reactive HIV-1-neutralizing antibodies...
- Characterization of a chimeric monoclonal antibody against the insulin-like growth factor-I receptorMei Yun Zhang
Center for Cancer Research Nanobiology Program, CCR, NCI Frederick, NIH, Frederick, MD, USA
MAbs 1:475-80. 2009..These results suggest that m590 could be an useful antibody in diagnosis and treatment of cancer, as well as a research tool...
- Improved breadth and potency of an HIV-1-neutralizing human single-chain antibody by random mutagenesis and sequential antigen panningMei Yun Zhang
Human Immunovirology and Computational Biology Group, LECB, CCR, National Cancer Institute-Frederick, NIH, Frederick, MD 21702, USA
J Mol Biol 335:209-19. 2004....
- Crystal structure of the broadly cross-reactive HIV-1-neutralizing Fab X5 and fine mapping of its epitopeRamalakshmi Darbha
Macromolecular Crystallography Laboratory, National Cancer Institute, Frederick, Maryland 21702, USA
Biochemistry 43:1410-7. 2004..The X5 structure and fine mapping of its epitope may assist in the elucidation of the mechanisms of viral entry and neutralization, and the development of HIV-1 inhibitors and vaccines...
- Structural basis of tyrosine sulfation and VH-gene usage in antibodies that recognize the HIV type 1 coreceptor-binding site on gp120Chih-chin Huang
Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
Proc Natl Acad Sci U S A 101:2706-11. 2004..When confronted by extraordinary viral defenses, the immune system unveils novel adaptive capabilities, with tyrosine sulfation enhancing the vocabulary of antigen recognition...
- Broadly cross-reactive HIV-1-neutralizing human monoclonal Fab selected for binding to gp120-CD4-CCR5 complexesMaxime Moulard
Department of Immunology, The Scripps Research Institute, La Jolla, CA 92037, USA
Proc Natl Acad Sci U S A 99:6913-8. 2002....
- Structure of a V3-containing HIV-1 gp120 coreChih Chin Huang
Vaccine Research Center, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892, USA
Science 310:1025-8. 2005..The extended nature and antibody accessibility of V3 explain its immunodominance. Together, the results provide a structural rationale for the role of V3 in HIV entry and neutralization...
- Recent advances in the characterization of HIV-1 neutralization assays for standardized evaluation of the antibody response to infection and vaccinationVictoria R Polonis
Walter Reed Army Institute of Research, Washington, DC, USA
Virology 375:315-20. 2008....
- Potent neutralization of Hendra and Nipah viruses by human monoclonal antibodiesZhongyu Zhu
CCRNP, CCR, NCI-Frederick, NIH, Frederick, MD 21702, USA
J Virol 80:891-9. 2006....
- Structural definition of a conserved neutralization epitope on HIV-1 gp120Tongqing Zhou
Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
Nature 445:732-7. 2007..A site of vulnerability, related to a functional requirement for efficient association with CD4, can therefore be targeted by antibody to neutralize HIV-1...
- Human monoclonal antibodies to the S glycoprotein and related proteins as potential therapeutics for SARSMei-Yun Zhang
National Institutes of Health, National Cancer Institute-Frederick, Center for Cancer Research, Laboratory of Experimental and Computational Biology, Protein Interactions Group, Frederick, MD 21702-1201, USA
Curr Opin Mol Ther 7:151-6. 2005..These antibodies potently neutralize infectious virus in tissue cultures and animal models, and, alone or in combination with vaccines and other drugs, may have potential for the prevention and treatment of SARS...