Mycobacterium tuberculosis produces pili during human infection

Christopher J. Alteri, Juan Xicohténcatl-Cortes, Sonja Hess, Guillermo Caballero-Olin, Jorge A. Girón, Richard L. Friedman

Research output: Contribution to journalArticlepeer-review

129 Scopus citations

Abstract

Mycobacterium tuberculosis is responsible for nearly 3 million human deaths worldwide every year. Understanding the mechanisms and bacterial factors responsible for the ability of M. tuberculosis to cause disease in humans is critical for the development of improved treatment strategies. Many bacterial pathogens use pili as adherence factors to colonize the host. We discovered that M. tuberculosis produces fine (2- to 3-nm-wide), aggregative, flexible pili that are recognized by IgG antibodies contained in sera obtained from patients with active tuberculosis, indicating that the bacilli produce pili or pili-associated antigen during human infection. Purified M. tuberculosis pili (MTP) are composed of low-molecular-weight protein subunits encoded by the predicted M. tuberculosis H37Rv ORF, designated Rv3312A. MTP bind to the extracellular matrix protein laminin in vitro, suggesting that MTP possess adhesive properties. Isogenic mtp mutants lost the ability to produce Mtp in vitro and demonstrated decreased laminin-binding capabilities. MTP shares morphological, biochemical, and functional properties attributed to bacterial pili, especially with curli amyloid fibers. Thus, we propose that MTP are previously unidentified host-colonization factors of M. tuberculosis.

Original languageEnglish (US)
Pages (from-to)5145-5150
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume104
Issue number12
DOIs
StatePublished - Mar 20 2007

Keywords

  • Adherence
  • Amyloid
  • Antigen
  • Laminin

ASJC Scopus subject areas

  • General

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