NDLI: Characterization of the Fibrinogen Binding Domain of Bacteriophage Lysin from Streptococcus mitis ▿

Content Provider	PubMed Central
Author	Seo, Ho Seong Sullam, Paul M.
Editor	Weiser, J. N.
Copyright Year	2011
Abstract	The binding of bacteria to human platelets is a likely central mechanism in the pathogenesis of infective endocarditis. Platelet binding by Streptococcus mitis SF100 is mediated in part by a lysin encoded by the lysogenic bacteriophage SM1. In addition to its role in the phage life cycle, lysin mediates the binding of S. mitis to human platelets via its interaction with fibrinogen on the platelet surface. To better define the region of lysin mediating fibrinogen binding, we tested a series of purified lysin truncation variants for their abilities to bind this protein. These studies revealed that the fibrinogen binding domain of lysin is contained within the region spanned by amino acid residues 102 to 198 (lysin102–198). This region has no sequence homology to other known fibrinogen binding proteins. Lysin102–198 bound fibrinogen comparably to full-length lysin and with the same selectivity for the fibrinogen Aα and Bβ chains. Lysin102–198 also inhibited the binding in vitro of S. mitis to human fibrinogen and platelets. When assessed by platelet aggregometry, the disruption of the lysin gene in SF100 resulted in a significantly longer time to the onset of aggregation of human platelets than that of the parent strain. The preincubation of platelets with purified lysin102–198 also delayed the onset of aggregation by SF100. These results indicate that the binding of lysin to fibrinogen is mediated by a specific domain of the phage protein and that this interaction is important for both platelet binding and aggregation by S. mitis.
Related Links	http://dx.doi.org/10.1128/iai.05088-11
Ending Page	3526
Page Count	9
Starting Page	3518
File Format	PDF
ISSN	00199567
e-ISSN	10985522
Journal	Infection and Immunity
Issue Number	9
Volume Number	79
Language	English
Publisher	American Society for Microbiology
Publisher Date	2011-09-01
Access Restriction	Open
Rights Holder	American Society for Microbiology
Subject Keyword	Immunology Microbiology Parasitology Infectious Diseases Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Infectious Diseases Parasitology Immunology Microbiology

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Characterization of the Fibrinogen Binding Domain of Bacteriophage Lysin from Streptococcus mitis (2011)

Bacteriophage Lysin Mediates the Binding of Streptococcus mitis to Human Platelets through Interaction with Fibrinogen

Bacteriophage lysin mediates the binding of streptococcus mitis to human platelets through interaction with fibrinogen.

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Characterization of the Fibrinogen Binding Domain of Bacteriophage Lysin from Streptococcus mitis ▿