PMID: 7888225Dec 1, 1994Paper

Characterization of monoclonal antibodies to human immunodeficiency virus type 2 envelope glycoproteins

AIDS Research and Human Retroviruses
F TraincardS Benichou

Abstract

Twelve murine monoclonal antibodies (MAbs) to human immunodeficiency virus type 2 (isolate ROD) envelope glycoproteins have been generated and characterized. Nine MAbs were specific to the external gp125 and three reacted with the transmembrane gp36. A large majority of MAbs displayed a significant affinity for the native gp140 precursor and were shown to bind to viral antigens on the surface of fixed HIV-2-infected cells. In Western blot analysis, the 12 MAbs showed varying profiles of cross-reactivity, but none of the MAbs cross-reacted with the HIV-1LAI envelope. Six MAbs reacted exclusively with the homologous HIV-2ROD isolate whereas only two MAbs displayed cross-reactivity with HIV-2ROD, HIV-2EHO, and SIVmac251. The four other MAbs cross-reacted with either HIV-2EHO or SIVmac251. Results of competitive binding assays indicated that the three anti-gp36 MAbs shared the same competition group, whereas at least eight competition groups were defined with the nine anti-gp125 MAbs. The epitopes of the three anti-gp36 and four anti-gp125 MAbs have been delineated using synthetic peptides or by immunological screening of an SIVmac251 peptide library expressed in yeast. The anti-gp36 MAbs are directed against the same domain of the...Continue Reading

References

Sep 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·H TowbinJ Gordon
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Feb 18, 1988·Nature·H W KestlerR C Desrosiers

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Citations

Nov 13, 2009·Journal of Peptide Science : an Official Publication of the European Peptide Society·Fabrice GastonElmostafa Bahraoui
Sep 18, 2008·The Journal of General Virology·Sansanee NoisakranNopporn Sittisombut
May 30, 1998·The Journal of Peptide Research : Official Journal of the American Peptide Society·B Belhadj Jrad, E Bahraoui

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