Direct interaction of complement factor H with the C1 domain of HIV type 1 glycoprotein 120. NLM AIDSLINE Important note: Information in this article was accurate in 1996. The state of the art may have changed since the publication date.

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Direct interaction of complement factor H with the C1 domain of HIV type 1 glycoprotein 120.

AIDS Res Hum Retroviruses. 1995 May;11(5):577-88. Unique Identifier : AIDSLINE MED/96093893
Pinter C; Siccardi AG; Longhi R; Clivio A; Dipartimento di Biologia e Genetica per le Scienze Mediche,; Universita di Milano, Milan, Italy.

Abstract: A protein that binds specifically to Env 105-119 (HEDIISLWDQSLKPC) was found in pools of normal human plasma when this peptide was used in affinity chromatography procedures. These samples represented the negative control in experiments aimed at the purification of putative human antibodies to the Env 105-119 region from AIDS sera. In this article we describe the biochemical characterization of this protein, which turned out to be complement factor H (CFH). We propose a functional role for this protein in the complex, early steps of CD4-dependent HIV infection.
Keywords: Amino Acid Sequence Chromatography, Ion Exchange Complement Factor H/ISOLATION & PURIF/*METABOLISM Giant Cells/VIROLOGY Human HIV Antibodies/IMMUNOLOGY HIV Envelope Protein gp120/IMMUNOLOGY/*METABOLISM HIV Envelope Protein gp41/METABOLISM HIV-1/IMMUNOLOGY/*METABOLISM Molecular Sequence Data Protein Binding Receptors, HIV/METABOLISM Support, Non-U.S. Gov't JOURNAL ARTICLEKWDaminoacidsequencechromatography,ionexchangecomplementfactorh/isolation&purif/KWDmetabolismgiantcells/virologyhumanhivantibodies/immunologyhivenvelopeproteingp120/immunology/KWDmetabolismhivenvelopeproteingp41/metabolismhiv-1/immunology/KWDmetabolismmolecularsequencedataproteinbindingreceptors,hiv/metabolismsupport,non-uKWDsKWDgov'tjournalarticle
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M9621035

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