Document 0002
 DOCN  M9460002
 TI    Interaction of C1 with HIV-1.
 DT    9408
 AU    Thielens NM; Bally IM; Ebenbichler CF; Dierich MP; Arlaud GJ; Institut
       de Biologie Structurale, Laboratire d'Enzymologie; Moleculaire,
       Grenoble, France.
 SO    Behring Inst Mitt. 1993 Dec;(93):165-70. Unique Identifier : AIDSLINE
       MED/94226564
 AB    In contrast to animal retroviruses such as murine leukemia virus, HIV-1
       is not lysed by human complement. Nevertheless, HIV-1 activates
       complement via the classical pathway independently of antibody. Evidence
       is provided for activation of the reconstituted C1 complex by the virus,
       resulting from direct interaction between C1q and the external part of
       the viral transmembrane envelope protein (sgp41). Using C1q fragments
       and synthetic peptides covering the putative interaction regions in C1q
       and sgp41, we obtain evidence that the C1q/HIV-1 interaction involves: A
       site on C1q that appears to be located in the intermediary region
       between the collagen-like and the globular regions of C1q, and which may
       be conformational, involving two or more C1q chains. A site on gp41
       located between residues 601 and 613 (gp160 nomenclature), i.e. within
       the immunodominant domain of HIV-1. This site shares homology with the
       corresponding region of HIV-2.
 DE    Amino Acid Sequence  Binding Sites  *Complement Pathway, Classical
       Complement 1/DRUG EFFECTS/METABOLISM/*PHYSIOLOGY  Human  HIV Envelope
       Protein gp41/DRUG EFFECTS/*METABOLISM  HIV-1/METABOLISM/*PHYSIOLOGY
       Kinetics  Molecular Sequence Data  Peptides/CHEMICAL
       SYNTHESIS/PHARMACOLOGY  Recombinant Proteins/METABOLISM  JOURNAL ARTICLE

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