Hybridoma Antibodies to the Lipid-Binding Site(S) in the Amino-Terminal Region of Fibronectin Inhibits Binding of Streptococcal Lipoteichoic Acid

Lena Stanislawski, Harry S. Courtney, W. Andrew Simpson, David L. Hasty, Edwin H. Beachey, L. Robert, Itzhak Ofek

Research output: Contribution to journalArticlepeer-review

Abstract

In this report, we present evidence to suggest that streptococci and lipoteichoic acid (LTA) interact with a fatty acid binding site located near the NH2-terminus of fibronectin. The evidence is based on the following observations. (1) Antibodies directed against a synthetic peptide (residues 1–30 of the amino-terminus of fibronectin) reacted with the two thermolysin-generated peptides (24 and 28 kilodaltons [kDa)) that were adsorbed by and eluted from streptococci. (2) The adsorption of the 24- and 28-kDa peptides to streptococci was inhibited by LTA. (3) The two monoclonal antibodies that inhibited the binding of LTA to fibronectin reacted only with the 24- and 28-kDA fragments of fibronectin. (4) Conversely, LTA, as well as lauric acid and oleic acid, blocked the binding of the same monoclonal antibodies to fibronectin. (5) LTA had no effect on the binding of hybridoma antibodies directed against the collagen or cell-binding domain.

Original languageEnglish
Pages (from-to)344-349
Number of pages6
JournalJournal of Infectious Diseases
Volume156
Issue number2
DOIs
StatePublished - Aug 1987

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