+ Site Statistics
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on Google+Follow on Google+
Follow on LinkedInFollow on LinkedIn

+ Translate

Treponema pallidum receptor binding proteins interact with fibronectin

Journal of Experimental Medicine 157(6): 1958-1970

Treponema pallidum receptor binding proteins interact with fibronectin

Analysis of plasma proteins avidly bound to T. pallidum surfaces revealed the ability of T. pallidum to acquire numerous host macromolecules. No acquisition was evident by the avirulent spirochete, T. phagedenis biotype Reiter. Western blotting technology using hyperimmune antifibronectin serum as a probe revealed the ability of virulent treponemes to avidly bind fibronectin from a complex medium such as plasma. The specificity of the tiplike adherence of motile T. pallidum to fibronectin-coated glass surfaces and to fibronectin on human laryngeal carcinoma HEp-2 cells was reinforced by the observation that pretreatment of coverslips or cell monolayers with monospecific antiserum against fibronectin substantially reduced T. pallidum attachment. The stoichiometric binding of T. pallidum to fibronectin-coated coverslips and the inability of unlabeled or 35S-radiolabeled treponemes to interact with glass surfaces treated with other plasma proteins further established the specific nature of the interaction between virulent T. pallidum and fibronectin. The avid association between 3 outer envelope proteins of T. pallidum and fibronectin was also demonstrated. These treponemal surface proteins have been previously identified as putative receptor-binding proteins responsible for T. pallidum parasitism of host cells. The data suggest that surface fibronectin mediates tip-oriented attachment of T. pallidum to host cells via a receptor-ligand mechanism of recognition.

Accession: 006839634

PMID: 6304227

DOI: 10.1084/jem.157.6.1958

Download PDF Full Text: Treponema pallidum receptor binding proteins interact with fibronectin

Related references

Treponema pallidum fibronectin-binding proteins. Journal of Bacteriology 186(20): 7019-7022, 2004

Molecular cloning of Treponema pallidum outer envelope fibronectin binding proteins, P1 and P2. Genitourinary Medicine 63(6): 355-360, 1987

Identification of lactoferrin-binding proteins from Treponema pallidum subspecies pallidum and Treponema denticola. Molecular Microbiology. 12(4): 613-619, 1994

Fibronectin mediated adherence of treponema pallidum is duplicated by fibronectin cell binding domain. Abstracts of the Annual Meeting of the American Society for Microbiology 85: 23, 1985

Fibronectin mediates Treponema pallidum cytadherence through recognition of fibronectin cell-binding domain. Journal of Experimental Medicine 161(3): 514-525, 1985

Antibody responses elicited against the Treponema pallidum repeat proteins differ during infection with different isolates of Treponema pallidum subsp. pallidum. Infection and Immunity 71(10): 6054-6057, 2003

Fibronectin binding to treponema pallidum. Journal of Cellular Biochemistry Supplement (8 PART B): 297, 1984

Molecular characterization of receptor binding proteins and immunogens of virulent Treponema pallidum. Journal of Experimental Medicine 151(3): 573-586, 1980

Penicillin binding proteins and peptidoglycan of treponema pallidum ssp pallidum. Infection & Immunity 57(4): 1248-1254, 1989

Homology among the amino terminal sequences of the multiple flagellar proteins of treponema pallidum ssp pallidum and treponema phagedenis kazan 5. Abstracts of the Annual Meeting of the American Society for Microbiology 88: 104, 1988