Skip to main content

Main menu

  • Home
  • Articles
    • Newest Articles
    • Current Issue
    • Archive
    • Subject Collections
    • Meeting Collections
  • Reviews & Opinions
    • Editorials
    • Insights
    • Perspectives
    • Reviews
  • Alerts
  • About
    • History
    • Editors & Staff
    • Policies & Permissions
    • Advertise
    • Contact Us
  • Submit
    • Submit a Manuscript
    • Instructions for Authors
    • Publication Fees
    • Author Services
  • Subscriptions
  • Rockefeller University Press
  • JCB
  • JEM
  • JGP
  • LSA

User menu

  • Log in

Search

  • Advanced search
JEM
  • Rockefeller University Press
  • JCB
  • JEM
  • JGP
  • LSA
  • Log in
JEM

Advanced Search

  • Home
  • Articles
    • Newest Articles
    • Current Issue
    • Archive
    • Subject Collections
    • Meeting Collections
  • Reviews & Opinions
    • Editorials
    • Insights
    • Perspectives
    • Reviews
  • Alerts
  • About
    • History
    • Editors & Staff
    • Policies & Permissions
    • Advertise
    • Contact Us
  • Submit
    • Submit a Manuscript
    • Instructions for Authors
    • Publication Fees
    • Author Services
  • Subscriptions

You are here

jem Home » 1977 Archive » 1 November » 146 (5): 1169
Article

Hemagglutination by purified type I Escherichia coli pili.

I E Salit, E C Gotschlich
I E Salit
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
E C Gotschlich
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
DOI: 10.1084/jem.146.5.1169 | Published November 1, 1977
  • Article
  • Info
  • Metrics
  • Preview PDF
Loading

Abstract

Many enterobacteria can cause agglutination of erythrocytes, but previous investigations have not proven which components of the bacteria are responsible. We used a strain of Escherichia coli K12 which causes mannose-sensitive hemagglutination (HA) of guinea pig cells. Common pili were purified from these bacteria by shearing them from the bacteria followed by selective precipitation in acid and ammonium sulfate. Isopycnic centrifugation in cesium chloride removed the remaining outer membrane protein contaminants. These pili are pure by electron microscopy and gel electrophoresis. By amino acid analysis, they have a mol wt of 17,099 and consist of 45% nonpolar residues. These purified pili agglutinate guinea pig erythrocytes, a reaction that is inhibited by anti-pili antibodies and by saccharides related in structure to D-mannose. Proteolytic treatment of erythrocytes does not diminish HA but rather increases the pili-induced HA of human cells. Neuraminidase enhances HA and mannosidase slightly diminishes it. It is concluded that purified pili alone cause HA of erythrocytes by binding to mannose-like molecules on the erythrocyte surface. Thus HA by bacterial pili serves as a useful model system for the mechanism of bacterial pili attachment ot cell membranes.

© 1977 Rockefeller University Press
Previous articleNext article
Back to top
Download PDF
Citation Tools
Hemagglutination by purified type I Escherichia coli pili.
I E Salit, E C Gotschlich
Journal of Experimental Medicine Nov 1977, 146 (5) 1169-1181; DOI: 10.1084/jem.146.5.1169

Citation Manager Formats

  • BibTeX
  • Bookends
  • EasyBib
  • EndNote (tagged)
  • EndNote 8 (xml)
  • Medlars
  • Mendeley
  • Papers
  • RefWorks Tagged
  • Ref Manager
  • RIS
  • Zotero
Alerts
Sign In to Email Alerts with your Email Address

Email logo Twitter logo Facebook logo Mendeley logo Reddit logo CiteULike logo LinkedIn logo
The Journal of Experimental Medicine: 215 (4)

Current Issue

April 2, 2018
Volume 215, No. 4

  • Table of Contents
  • All Issues

Jump To

  • Article
  • Info
  • Metrics
  • Preview PDF
 

ARTICLES

  • Current Issue
  • Newest Articles
  • Archive
  • Alerts
  • RSS feeds

FOR AUTHORS

  • Submit a Manuscript
  • Instructions for Authors

ABOUT

  • About JEM
  • Editors & Staff
  • Policies & Permissions
  • Advertise
  • Contact Us
  • Feedback
  • Newsroom

CONNECT WITH JEM

  • Email
  • Facebook
  • Twitter
  • RSS
  • Instagram

Online ISSN: 1540-9538
Print ISSN: 0022-1007

Copyright © 2018 JEM by Rockefeller University Press