Characterization of V3 loop-binding protein(s) of Molt-4 and U937 cells.

Important note: Information in this article was accurate in 1996. The state of the art may have changed since the publication date.

Characterization of V3 loop-binding protein(s) of Molt-4 and U937 cells.

AIDS Res Hum Retroviruses. 1995 May;11(5):563-70. Unique Identifier : AIDSLINE MED/96093891
Xu Y; Murakami T; Kawase S; Uchiyama T; Hattori T; Laboratory for AIDS Immunology, Kyoto University, Japan.

Abstract: The V3 loop in gp120 of human immunodeficiency virus type 1 (HIV-1) is known as a principal neutralizing and cell-tropic determinant. Biotinylated synthetic V3 loop peptides derived from three different HIV-1 strains were used as ligands to identify the cell surface counterreceptor, which may participate in the infection of HIV-1. Two different cell lines, Molt-4 and U937, and three V3 loop peptides derived from LAVELI, HTLV-IIIMN, and HTLV-IIIB strains were used. The binding of HTLV-IIIB-derived peptide to the cell surface was confirmed using 125I-labeled surface proteins of both cell lines. The relative molecular mass of the major radioactive band on the autoradiogram was 32-33 kDa in both cell lines. A protein was purified from the plasma membrane fraction of Molt-4 cells using affinity columns coupled with three different V3 loop peptides. Two major polypeptides (32 and 33 kDa) were eluted from the affinity column. Size-exclusion chromatography showed that the protein migrated as a single peak with a molecular mass of 130 kDa. These proteins were separated by reversed-phase chromatography, which indicated that the 32-kDa protein is more hydrophobic than the 33-kDa protein in Molt-4 cells. A similar but not identical 130-kDa protein with 32- and 33-kDa polypeptides were also purified from U937 cells. These findings indicate that HIV-1 utilizes a tetrameric protein on the surface of Molt-4 and U937 cells on infection.

Keywords: Amino Acid Sequence Chromatography, Affinity Chromatography, High Pressure Liquid CD4-Positive T-Lymphocytes/METABOLISM/VIROLOGY Human HIV Envelope Protein gp120/*METABOLISM HIV-1/*METABOLISM Molecular Sequence Data Peptide Fragments/*METABOLISM Protein Binding Receptors, HIV/ISOLATION & PURIF/*METABOLISM Support, Non-U.S. Gov't Tumor Cells, Cultured JOURNAL ARTICLE
960228
M9621037

AEGiS is a 501(c)3, not-for-profit, tax-exempt, educational corporation. AEGiS is made possible through unrestricted funding from Boehringer Ingelheim, Bridgestone/Firestone Charitable Trust, Bristol-Myers Squibb Company, Elton John AIDS Foundation, Gill Foundation, the National Library of Medicine, Quest Diagnostics, Roche and Trimeris, and donations from users like you. Always watch for outdated information. This article first appeared in 1996. This material is designed to support, not replace, the relationship that exists between you and your doctor.

AEGiS presents published material, reprinted with permission and neither endorses nor opposes any material. All information contained on this website, including information relating to health conditions, products, and treatments, is for informational purposes only. It is often presented in summary or aggregate form. It is not meant to be a substitute for the advice provided by your own physician or other medical professionals. Always discuss treatment options with a doctor who specializes in treating HIV.

Copyright ©1980, 1996. AEGiS. All materials appearing on AEGiS are protected by copyright as a collective work or compilation under U.S. copyright and other laws and are the property of AEGiS, or the party credited as the provider of the content. .