Lipoteichoic acid-binding and biological properties of T protein of group A Streptococcus

R. H. Johnson, W. A. Simpson, James Dale, I. Ofek, E. H. Beachey

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

T protein was extracted with trypsin from an avirulent, M protein-deficient, type 1 group A Streptococcus and purified by ammonium sulfate precipitation and anion-exchange chromatography. The latter procedure removed contaminating lipoteichoic acid (LTA) from the T protein, which consisted of a heterogeneous mixture of polypeptides resistant to digestion by trypsin and ranged in molecular size from 160,000 to 200,000 daltons. Threonine, aspartic acid, glutamic acid, lysine, and valine were the most predominant amino acids. The binding of LTA to an affinity column of T protein was reversible with increasing concentrations of ethanol but not with increasing ionic strength. T protein bound less palmitic acid and LTA than did fatty acid-free bovine albumin and did not stimulate human peripheral lymphocytes. Because the surface and cell wall distribution of the T proteins and LTA appear similar, the possibility exists that T proteins and LTA may interact in situ by weakly hydrophobic bonds. Such ligand-ligand interaction may be indirectly involved in the adherence of group A streptococci to host cell membranes that is known to be mediated by LTA.

Original languageEnglish (US)
Pages (from-to)791-798
Number of pages8
JournalInfection and Immunity
Volume29
Issue number2
StatePublished - Oct 27 1980
Externally publishedYes

Fingerprint

Streptococcus
Proteins
Trypsin
Ligands
Palmitic Acid
Valine
Ammonium Sulfate
Threonine
lipoteichoic acid
Nonesterified Fatty Acids
Aspartic Acid
Osmolar Concentration
Cell Wall
Lysine
Anions
Chromatography
Glutamic Acid
Digestion
Albumins
Ethanol

All Science Journal Classification (ASJC) codes

  • Parasitology
  • Microbiology
  • Immunology
  • Infectious Diseases

Cite this

Johnson, R. H., Simpson, W. A., Dale, J., Ofek, I., & Beachey, E. H. (1980). Lipoteichoic acid-binding and biological properties of T protein of group A Streptococcus. Infection and Immunity, 29(2), 791-798.

Lipoteichoic acid-binding and biological properties of T protein of group A Streptococcus. / Johnson, R. H.; Simpson, W. A.; Dale, James; Ofek, I.; Beachey, E. H.

In: Infection and Immunity, Vol. 29, No. 2, 27.10.1980, p. 791-798.

Research output: Contribution to journalArticle

Johnson, RH, Simpson, WA, Dale, J, Ofek, I & Beachey, EH 1980, 'Lipoteichoic acid-binding and biological properties of T protein of group A Streptococcus', Infection and Immunity, vol. 29, no. 2, pp. 791-798.
Johnson, R. H. ; Simpson, W. A. ; Dale, James ; Ofek, I. ; Beachey, E. H. / Lipoteichoic acid-binding and biological properties of T protein of group A Streptococcus. In: Infection and Immunity. 1980 ; Vol. 29, No. 2. pp. 791-798.
@article{26d93a8a4cd74b21a59d24fccb6da623,
title = "Lipoteichoic acid-binding and biological properties of T protein of group A Streptococcus",
abstract = "T protein was extracted with trypsin from an avirulent, M protein-deficient, type 1 group A Streptococcus and purified by ammonium sulfate precipitation and anion-exchange chromatography. The latter procedure removed contaminating lipoteichoic acid (LTA) from the T protein, which consisted of a heterogeneous mixture of polypeptides resistant to digestion by trypsin and ranged in molecular size from 160,000 to 200,000 daltons. Threonine, aspartic acid, glutamic acid, lysine, and valine were the most predominant amino acids. The binding of LTA to an affinity column of T protein was reversible with increasing concentrations of ethanol but not with increasing ionic strength. T protein bound less palmitic acid and LTA than did fatty acid-free bovine albumin and did not stimulate human peripheral lymphocytes. Because the surface and cell wall distribution of the T proteins and LTA appear similar, the possibility exists that T proteins and LTA may interact in situ by weakly hydrophobic bonds. Such ligand-ligand interaction may be indirectly involved in the adherence of group A streptococci to host cell membranes that is known to be mediated by LTA.",
author = "Johnson, {R. H.} and Simpson, {W. A.} and James Dale and I. Ofek and Beachey, {E. H.}",
year = "1980",
month = "10",
day = "27",
language = "English (US)",
volume = "29",
pages = "791--798",
journal = "Infection and Immunity",
issn = "0019-9567",
publisher = "American Society for Microbiology",
number = "2",

}

TY - JOUR

T1 - Lipoteichoic acid-binding and biological properties of T protein of group A Streptococcus

AU - Johnson, R. H.

AU - Simpson, W. A.

AU - Dale, James

AU - Ofek, I.

AU - Beachey, E. H.

PY - 1980/10/27

Y1 - 1980/10/27

N2 - T protein was extracted with trypsin from an avirulent, M protein-deficient, type 1 group A Streptococcus and purified by ammonium sulfate precipitation and anion-exchange chromatography. The latter procedure removed contaminating lipoteichoic acid (LTA) from the T protein, which consisted of a heterogeneous mixture of polypeptides resistant to digestion by trypsin and ranged in molecular size from 160,000 to 200,000 daltons. Threonine, aspartic acid, glutamic acid, lysine, and valine were the most predominant amino acids. The binding of LTA to an affinity column of T protein was reversible with increasing concentrations of ethanol but not with increasing ionic strength. T protein bound less palmitic acid and LTA than did fatty acid-free bovine albumin and did not stimulate human peripheral lymphocytes. Because the surface and cell wall distribution of the T proteins and LTA appear similar, the possibility exists that T proteins and LTA may interact in situ by weakly hydrophobic bonds. Such ligand-ligand interaction may be indirectly involved in the adherence of group A streptococci to host cell membranes that is known to be mediated by LTA.

AB - T protein was extracted with trypsin from an avirulent, M protein-deficient, type 1 group A Streptococcus and purified by ammonium sulfate precipitation and anion-exchange chromatography. The latter procedure removed contaminating lipoteichoic acid (LTA) from the T protein, which consisted of a heterogeneous mixture of polypeptides resistant to digestion by trypsin and ranged in molecular size from 160,000 to 200,000 daltons. Threonine, aspartic acid, glutamic acid, lysine, and valine were the most predominant amino acids. The binding of LTA to an affinity column of T protein was reversible with increasing concentrations of ethanol but not with increasing ionic strength. T protein bound less palmitic acid and LTA than did fatty acid-free bovine albumin and did not stimulate human peripheral lymphocytes. Because the surface and cell wall distribution of the T proteins and LTA appear similar, the possibility exists that T proteins and LTA may interact in situ by weakly hydrophobic bonds. Such ligand-ligand interaction may be indirectly involved in the adherence of group A streptococci to host cell membranes that is known to be mediated by LTA.

UR - http://www.scopus.com/inward/record.url?scp=0018947176&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0018947176&partnerID=8YFLogxK

M3 - Article

VL - 29

SP - 791

EP - 798

JO - Infection and Immunity

JF - Infection and Immunity

SN - 0019-9567

IS - 2

ER -