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Interaction of the envelope clycoprotein of human immunodeficiency virus with C1Q and fibronectin...

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Interaction of the envelope clycoprotein of human immunodeficiency virus with C1Q and fibronectin under the low ionic strength conditions present in human saliva

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Title	Interaction of the envelope clycoprotein of human immunodeficiency virus with C1Q and fibronectin under the low ionic strength conditions present in human saliva
Author	Su, Helene
Date	1991
Affiliation/College	College of Graduate Studies
Department	Microbiology and Immunology
Extent	iii, 252 leaves : ill. ; 29 cm
Subject.MeSH	Saliva--microbiology HIV Envelope Protein gp120 Academic Dissertations
Collection	MUSC Theses and Dissertations
Contributing Institution	Waring Historical Library (MUSC)
Rights	Copyright is held by the author.
Language	English
Type	Text
Format	application/pdf
Media Type	Manuscripts
Resource Identifier	mtd1991_su_h
Abstract	Human saliva has been shown to reduce the infectivity of human immunodeficiency virus (HIV) particles in vitro (Fox et al., 1988). The factors in human saliva involved in this inhibition of HIV infectivity are unknown, although the salivary sediment of normal individuals has the major HIV neutralizing activity (Fox et al., 1989). Interestingly, the first complement component (Cl) has been detected on the surface of the salivary sediment in the whole saliva of normal individuals (Wirtz et al., 1987). We determined that at the low ionic strength of saliva, human Clq bound with high affinity to the envelope glycoprotein of HIV (Su and Boackle, 1991). Normally, the interaction of the Clq globular heads with immune complexes causes Cl activation. However, direct interactions between Cl and rgp120 (or rgp160) did not lead to Cl fixation, as determined by hemolytic studies with rate limiting levels of Cl, nor did rgpl20 cause Cl activation (as determined by the formation of CroCI-Inh complexes or by activated CIs mediated C4 conversion and subsequent C3 conversion in normal human serum). These latter findings infer that the Clq globular heads might not be involved in the interaction. Using ELISA, it was observed that macromolecular CI, with the Clr2Cls2 tetrarner associated with the collagen-like stem of Clq, did not bind to immobilized rgpl20, whereas free (dissociated) Clq did bind. In addition, digestion of the Clq stem portion with collagenase, completely eliminated its binding to rgp120. These findings suggested that the collagen-like stem region of Clq, rather than the globular heads, participated in the binding to the envelope glycoprotein of HIV. Fibronectin, which is present in submandibular saliva, appeared to bind to rgp120 and enhanced the interaction of Clq with rgp120. It is conceivable that Clq and fibronectin, in binding and sequestering HIV particles (i.e. to the salivary sediment) may play an important role in the reduction of HIV transmission via saliva.

Interaction of the envelope clycoprotein of human immunodeficiency virus with C1Q and fibronectin under the low ionic strength conditions present in human saliva

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