Attachment of mycoplasmas to erythrocytes: A model to study mycoplasma attachment to the epithelium of the host respiratory tract

I. Kahane, S. Pnini, M. Banai, J. B. Baseman, G. H. Cassell, W. Bredt

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Mycoplasma pneumoniae, M. gallisepticum and M. pulmonis are pathogens of the respiratory tract. Their adherence to the host tissue is a prerequisite for manifestation of the disease. The attachment occurs between membrane components of the mycoplasmas and the host cells. In the attachment of M. pneumoniae and M. gallisepticum, binding sites of a protein nature of the mycoplasma membranes interact primarily with sialic acid residues of sialoglycoproteins of the host cell membranes. The latter was clearly indicated in studies on the pathogenic strain of M. pneumoniae and its nonpathogenic nonhemadsorbing mutants, and by the assessment of the direct binding of glycophorin [the major sialoglycoprotein of human red blood cells (RBC)] and other sialoglycoproteins to M. pneumoniae and M. gallisepticum. The components involved in the interaction of M. pulmonis with the host cells are not as well characterized, since the attachment is not affected by proteolytic treatment of the mycoplasmas, nor by removal of sialic acid residues from the host cell membranes. The attachment of the mycoplasmas to the host cells also occurs with nonviable organisms and can, in addition, be reproduced by isolated membranes. The binding sites of M. pneumoniae and M. gallisepticum were partially purified by affinity chromatography, using the high affinity of the binding sites for glycophorin. By this procedure the membranes were solubilized with detergents and chromatographed through glycophorin attached to Sepharose 4B as an affinity matrix. The binding sites retained the high affinity for glycophorin and bound to RBC membranes. Are the binding sites distributed throughout the membrane? Since the binding of the mycoplasma is via a polar structure (the tip or bleb), one may suggest that these structures harbor them. Experimental evidence for their distribution is being sought.

Original languageEnglish (US)
Pages (from-to)589-592
Number of pages4
JournalIsrael Journal of Medical Sciences
Volume17
Issue number7
StatePublished - 1981
Externally publishedYes

Fingerprint

Mycoplasma pneumoniae
Mycoplasma
Glycophorin
Binding sites
Respiratory System
Sialoglycoproteins
Epithelium
Erythrocytes
Binding Sites
Membranes
Cell membranes
Cell Membrane
N-Acetylneuraminic Acid
Blood
Affinity chromatography
Acids
Detergents
Pathogens
Blister
Ports and harbors

ASJC Scopus subject areas

  • Bioengineering
  • Medicine(all)

Cite this

Attachment of mycoplasmas to erythrocytes : A model to study mycoplasma attachment to the epithelium of the host respiratory tract. / Kahane, I.; Pnini, S.; Banai, M.; Baseman, J. B.; Cassell, G. H.; Bredt, W.

In: Israel Journal of Medical Sciences, Vol. 17, No. 7, 1981, p. 589-592.

Research output: Contribution to journalArticle

Kahane, I. ; Pnini, S. ; Banai, M. ; Baseman, J. B. ; Cassell, G. H. ; Bredt, W. / Attachment of mycoplasmas to erythrocytes : A model to study mycoplasma attachment to the epithelium of the host respiratory tract. In: Israel Journal of Medical Sciences. 1981 ; Vol. 17, No. 7. pp. 589-592.
@article{9ef7e25371e54a2d8cece4c9a69a4906,
title = "Attachment of mycoplasmas to erythrocytes: A model to study mycoplasma attachment to the epithelium of the host respiratory tract",
abstract = "Mycoplasma pneumoniae, M. gallisepticum and M. pulmonis are pathogens of the respiratory tract. Their adherence to the host tissue is a prerequisite for manifestation of the disease. The attachment occurs between membrane components of the mycoplasmas and the host cells. In the attachment of M. pneumoniae and M. gallisepticum, binding sites of a protein nature of the mycoplasma membranes interact primarily with sialic acid residues of sialoglycoproteins of the host cell membranes. The latter was clearly indicated in studies on the pathogenic strain of M. pneumoniae and its nonpathogenic nonhemadsorbing mutants, and by the assessment of the direct binding of glycophorin [the major sialoglycoprotein of human red blood cells (RBC)] and other sialoglycoproteins to M. pneumoniae and M. gallisepticum. The components involved in the interaction of M. pulmonis with the host cells are not as well characterized, since the attachment is not affected by proteolytic treatment of the mycoplasmas, nor by removal of sialic acid residues from the host cell membranes. The attachment of the mycoplasmas to the host cells also occurs with nonviable organisms and can, in addition, be reproduced by isolated membranes. The binding sites of M. pneumoniae and M. gallisepticum were partially purified by affinity chromatography, using the high affinity of the binding sites for glycophorin. By this procedure the membranes were solubilized with detergents and chromatographed through glycophorin attached to Sepharose 4B as an affinity matrix. The binding sites retained the high affinity for glycophorin and bound to RBC membranes. Are the binding sites distributed throughout the membrane? Since the binding of the mycoplasma is via a polar structure (the tip or bleb), one may suggest that these structures harbor them. Experimental evidence for their distribution is being sought.",
author = "I. Kahane and S. Pnini and M. Banai and Baseman, {J. B.} and Cassell, {G. H.} and W. Bredt",
year = "1981",
language = "English (US)",
volume = "17",
pages = "589--592",
journal = "Israel Medical Association Journal",
issn = "1565-1088",
publisher = "Israel Medical Association",
number = "7",

}

TY - JOUR

T1 - Attachment of mycoplasmas to erythrocytes

T2 - A model to study mycoplasma attachment to the epithelium of the host respiratory tract

AU - Kahane, I.

AU - Pnini, S.

AU - Banai, M.

AU - Baseman, J. B.

AU - Cassell, G. H.

AU - Bredt, W.

PY - 1981

Y1 - 1981

N2 - Mycoplasma pneumoniae, M. gallisepticum and M. pulmonis are pathogens of the respiratory tract. Their adherence to the host tissue is a prerequisite for manifestation of the disease. The attachment occurs between membrane components of the mycoplasmas and the host cells. In the attachment of M. pneumoniae and M. gallisepticum, binding sites of a protein nature of the mycoplasma membranes interact primarily with sialic acid residues of sialoglycoproteins of the host cell membranes. The latter was clearly indicated in studies on the pathogenic strain of M. pneumoniae and its nonpathogenic nonhemadsorbing mutants, and by the assessment of the direct binding of glycophorin [the major sialoglycoprotein of human red blood cells (RBC)] and other sialoglycoproteins to M. pneumoniae and M. gallisepticum. The components involved in the interaction of M. pulmonis with the host cells are not as well characterized, since the attachment is not affected by proteolytic treatment of the mycoplasmas, nor by removal of sialic acid residues from the host cell membranes. The attachment of the mycoplasmas to the host cells also occurs with nonviable organisms and can, in addition, be reproduced by isolated membranes. The binding sites of M. pneumoniae and M. gallisepticum were partially purified by affinity chromatography, using the high affinity of the binding sites for glycophorin. By this procedure the membranes were solubilized with detergents and chromatographed through glycophorin attached to Sepharose 4B as an affinity matrix. The binding sites retained the high affinity for glycophorin and bound to RBC membranes. Are the binding sites distributed throughout the membrane? Since the binding of the mycoplasma is via a polar structure (the tip or bleb), one may suggest that these structures harbor them. Experimental evidence for their distribution is being sought.

AB - Mycoplasma pneumoniae, M. gallisepticum and M. pulmonis are pathogens of the respiratory tract. Their adherence to the host tissue is a prerequisite for manifestation of the disease. The attachment occurs between membrane components of the mycoplasmas and the host cells. In the attachment of M. pneumoniae and M. gallisepticum, binding sites of a protein nature of the mycoplasma membranes interact primarily with sialic acid residues of sialoglycoproteins of the host cell membranes. The latter was clearly indicated in studies on the pathogenic strain of M. pneumoniae and its nonpathogenic nonhemadsorbing mutants, and by the assessment of the direct binding of glycophorin [the major sialoglycoprotein of human red blood cells (RBC)] and other sialoglycoproteins to M. pneumoniae and M. gallisepticum. The components involved in the interaction of M. pulmonis with the host cells are not as well characterized, since the attachment is not affected by proteolytic treatment of the mycoplasmas, nor by removal of sialic acid residues from the host cell membranes. The attachment of the mycoplasmas to the host cells also occurs with nonviable organisms and can, in addition, be reproduced by isolated membranes. The binding sites of M. pneumoniae and M. gallisepticum were partially purified by affinity chromatography, using the high affinity of the binding sites for glycophorin. By this procedure the membranes were solubilized with detergents and chromatographed through glycophorin attached to Sepharose 4B as an affinity matrix. The binding sites retained the high affinity for glycophorin and bound to RBC membranes. Are the binding sites distributed throughout the membrane? Since the binding of the mycoplasma is via a polar structure (the tip or bleb), one may suggest that these structures harbor them. Experimental evidence for their distribution is being sought.

UR - http://www.scopus.com/inward/record.url?scp=0019357809&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0019357809&partnerID=8YFLogxK

M3 - Article

C2 - 7287399

AN - SCOPUS:0019357809

VL - 17

SP - 589

EP - 592

JO - Israel Medical Association Journal

JF - Israel Medical Association Journal

SN - 1565-1088

IS - 7

ER -