1. The Importance of Antibody Isotype in HIV-1 Virus Capture Assay and in TZM-bl Neutralization.
- Author
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Kristina K. Peachman, Lindsay Wieczorek, Gary R. Matyas, Victoria R. Polonis, Carl R. Alving, and Mangala Rao
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MICROBIOLOGICAL assay , *IMMUNOGLOBULIN M , *MONOCLONAL antibodies , *PROTEIN binding , *HIV , *LABORATORY mice , *ENZYME-linked immunosorbent assay - Abstract
AbstractThe binding of murine IgM mAbs to five different clades of HIV-1 was examined using a modified ELISA-based virus capture assay. Two murine multispecific IgM mAbs that exhibit both lipid and gp41 epitope specificities, and one murine IgM mAb that exhibits lipid-binding specificity, were utilized. The binding of the IgG and the IgM isotypes of human mAb 2F5 to clades A through AE were also evaluated. The binding of 2F5 to HIV-1 was dependent upon the antibody isotype. Monoclonal IgM antibodies bound significantly lower amounts of HIV-1 than the corresponding IgG isotype. Although murine IgM mAbs bound HIV-1 to varying degrees in the virus capture assay, they failed to neutralize HIV-1 in a TZM-bl pseudovirus assay. In contrast, 2F5-IgM mAb bound certain HIV-1 isolates, and also neutralized them, although not as efficiently as the 2F5-IgG isotype. Studies on the relationship between virus binding and neutralization in a TZM-bl pseudovirus assay indicated that in most cases, mAbs that exhibited neutralization also bound the virus. [ABSTRACT FROM AUTHOR]
- Published
- 2010
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