A 28-kilodalton fibronectin-binding protein of group a streptococci

Harry Courtney, David L. Hasty, James Dale, Thomas P. Poirier

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

Lipoteichoic acid (LTA) has been implicated as a major adhesin of group A streptococci that interacts with fibronectin (Fn). It has been suggested that protein adhesins may also be involved in the binding of Fn to streptococci. We searched for such a protein by transblotting membrane preparations from M types 5, 19, and 24 group A streptococci to nitrocellulose and reacting the blot with125I-Fn. The Fn reacted with a 28-kDa polypeptide from all three serotypes of streptococci. Using affinity-purified antibodies to the 28-kDa protein in immunoblots of membrane preparations from various streptococci, we demonstrated that the 28-kDa protein is present in all 17 strains tested. Affinity-purified antibodies to the 28-kDa protein also reacted in varying degrees with intact streptococci, demonstrating that the antigen is exposed on the surface of intact organisms. Our results suggest that, in addition to LTA, group A streptococci contain a common Fn-binding moiety that is expressed as a major component of membrane preparations and that is accessible on the surface of streptococci for interactions with Fn.

Original languageEnglish (US)
Pages (from-to)245-250
Number of pages6
JournalCurrent Microbiology
Volume25
Issue number5
DOIs
StatePublished - Nov 1 1992

Fingerprint

Streptococcus
Fibronectins
Carrier Proteins
Antibody Affinity
Proteins
Collodion
Membranes
Membrane Proteins
Antigens
Peptides

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Applied Microbiology and Biotechnology

Cite this

A 28-kilodalton fibronectin-binding protein of group a streptococci. / Courtney, Harry; Hasty, David L.; Dale, James; Poirier, Thomas P.

In: Current Microbiology, Vol. 25, No. 5, 01.11.1992, p. 245-250.

Research output: Contribution to journalArticle

Courtney, Harry ; Hasty, David L. ; Dale, James ; Poirier, Thomas P. / A 28-kilodalton fibronectin-binding protein of group a streptococci. In: Current Microbiology. 1992 ; Vol. 25, No. 5. pp. 245-250.
@article{2720ff52ac184760b34c6564b958b782,
title = "A 28-kilodalton fibronectin-binding protein of group a streptococci",
abstract = "Lipoteichoic acid (LTA) has been implicated as a major adhesin of group A streptococci that interacts with fibronectin (Fn). It has been suggested that protein adhesins may also be involved in the binding of Fn to streptococci. We searched for such a protein by transblotting membrane preparations from M types 5, 19, and 24 group A streptococci to nitrocellulose and reacting the blot with125I-Fn. The Fn reacted with a 28-kDa polypeptide from all three serotypes of streptococci. Using affinity-purified antibodies to the 28-kDa protein in immunoblots of membrane preparations from various streptococci, we demonstrated that the 28-kDa protein is present in all 17 strains tested. Affinity-purified antibodies to the 28-kDa protein also reacted in varying degrees with intact streptococci, demonstrating that the antigen is exposed on the surface of intact organisms. Our results suggest that, in addition to LTA, group A streptococci contain a common Fn-binding moiety that is expressed as a major component of membrane preparations and that is accessible on the surface of streptococci for interactions with Fn.",
author = "Harry Courtney and Hasty, {David L.} and James Dale and Poirier, {Thomas P.}",
year = "1992",
month = "11",
day = "1",
doi = "10.1007/BF01575856",
language = "English (US)",
volume = "25",
pages = "245--250",
journal = "Current Microbiology",
issn = "0343-8651",
publisher = "Springer New York",
number = "5",

}

TY - JOUR

T1 - A 28-kilodalton fibronectin-binding protein of group a streptococci

AU - Courtney, Harry

AU - Hasty, David L.

AU - Dale, James

AU - Poirier, Thomas P.

PY - 1992/11/1

Y1 - 1992/11/1

N2 - Lipoteichoic acid (LTA) has been implicated as a major adhesin of group A streptococci that interacts with fibronectin (Fn). It has been suggested that protein adhesins may also be involved in the binding of Fn to streptococci. We searched for such a protein by transblotting membrane preparations from M types 5, 19, and 24 group A streptococci to nitrocellulose and reacting the blot with125I-Fn. The Fn reacted with a 28-kDa polypeptide from all three serotypes of streptococci. Using affinity-purified antibodies to the 28-kDa protein in immunoblots of membrane preparations from various streptococci, we demonstrated that the 28-kDa protein is present in all 17 strains tested. Affinity-purified antibodies to the 28-kDa protein also reacted in varying degrees with intact streptococci, demonstrating that the antigen is exposed on the surface of intact organisms. Our results suggest that, in addition to LTA, group A streptococci contain a common Fn-binding moiety that is expressed as a major component of membrane preparations and that is accessible on the surface of streptococci for interactions with Fn.

AB - Lipoteichoic acid (LTA) has been implicated as a major adhesin of group A streptococci that interacts with fibronectin (Fn). It has been suggested that protein adhesins may also be involved in the binding of Fn to streptococci. We searched for such a protein by transblotting membrane preparations from M types 5, 19, and 24 group A streptococci to nitrocellulose and reacting the blot with125I-Fn. The Fn reacted with a 28-kDa polypeptide from all three serotypes of streptococci. Using affinity-purified antibodies to the 28-kDa protein in immunoblots of membrane preparations from various streptococci, we demonstrated that the 28-kDa protein is present in all 17 strains tested. Affinity-purified antibodies to the 28-kDa protein also reacted in varying degrees with intact streptococci, demonstrating that the antigen is exposed on the surface of intact organisms. Our results suggest that, in addition to LTA, group A streptococci contain a common Fn-binding moiety that is expressed as a major component of membrane preparations and that is accessible on the surface of streptococci for interactions with Fn.

UR - http://www.scopus.com/inward/record.url?scp=0026490044&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026490044&partnerID=8YFLogxK

U2 - 10.1007/BF01575856

DO - 10.1007/BF01575856

M3 - Article

VL - 25

SP - 245

EP - 250

JO - Current Microbiology

JF - Current Microbiology

SN - 0343-8651

IS - 5

ER -