Immunotypes of a Quaternary Site of HIV-1 Vulnerability and Their Recognition by Antibodies | Zendy

Xueling Wu | Zendy; Anita Changela | Zendy; Sijy O’Dell | Zendy; Stephen D. Schmidt | Zendy; Marie Pancera | Zendy; Yongping Yang | Zendy; Baoshan Zhang | Zendy; Miroslaw K. Górny | Zendy; Sanjay Phogat | Zendy; James E. Robinson | Zendy; Leonidas Stamatatos | Zendy; Susan ZollaPazner | Zendy; Peter D. Kwong | Zendy; John R. Mascola | Zendy

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Immunotypes of a Quaternary Site of HIV-1 Vulnerability and Their Recognition by Antibodies

Author(s) -

Xueling Wu,

Anita Changela,

Sijy O’Dell,

Stephen D. Schmidt,

Marie Pancera,

Yongping Yang,

Baoshan Zhang,

Miroslaw K. Górny,

Sanjay Phogat,

James E. Robinson,

Leonidas Stamatatos,

Susan ZollaPazner,

Peter D. Kwong,

John R. Mascola

Publication year - 2011

Publication title -

journal of virology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.617

H-Index - 292

eISSN - 1070-6321

pISSN - 0022-538X

DOI - 10.1128/jvi.02585-10

Subject(s) - neutralization , biology , epitope , antibody , virology , protein quaternary structure , glycan , antigen , virus , immunology , genetics , protein subunit , glycoprotein , gene

HIV-1 is neutralized by a class of antibodies that preferentially recognize a site formed on the assembled viral spike. Such quaternary structure-specific antibodies have diverse neutralization breadths, with antibodies PG16 and PG9 able to neutralize 70 to 80% of circulating HIV-1 isolates while antibody 2909 is specific for strain SF162. We show that alteration between a rare lysine and a common N-linked glycan at position 160 of HIV-1 gp120 is primarily responsible for toggling between 2909 and PG16/PG9 neutralization sensitivity. Quaternary structure-specific antibodies appear to target antigenic variants of the same epitope, with neutralization breadth determined by the prevalence of recognized variants among circulating isolates.

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