Mycoplasma Pneumoniae Proteins That Selectively Bind to Host Cells

Overview

Journal Infect Immun

Publisher American Society for Microbiology

Specialty Allergy & Immunology

Date 1982 Jul 1

PMID 6809635

Citations 24

Authors

D C Krause

J B Baseman

Affiliations

Soon will be listed here.

Abstract

Mycoplasma pneumoniae proteins that bind to hamster trachea epithelial cells were identified by incubating 125I-labeled, detergent-solubilized mycoplasmas with glutaraldehyde-fixed host cells. Analysis of the bound fraction by gel electrophoresis and autoradiography revealed that proteins P1, P2, and HMW3 (molecular weights, 165,000, 110,000, and 140,000, respectively), previously implicated in attachment, were among the predominant species. Unlabeled mycoplasma preparations competed with the binding of radiolabeled proteins, suggesting the involvement of a limited number of receptor sites on the host cells.

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Processing is required for a fully functional protein P30 in Mycoplasma pneumoniae gliding and cytadherence.

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Functional domain analysis of the Mycoplasma pneumoniae co-chaperone TopJ.

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