Legionella pneumophila secretes an endoglucanase that belongs to the family-5 of glycosyl hydrolases and is dependent upon type II secretion

Meghan M. Pearce, Nicholas P. Cianciotto

Research output: Contribution to journalArticlepeer-review

30 Scopus citations

Abstract

Examination of cell-free culture supernatants revealed that Legionella pneumophila strains secrete an endoglucanase activity. Legionella pneumophila lspF mutants were deficient for this activity, indicating that the endoglucanase is secreted by the bacterium's type II protein secretion (T2S) system. Inactivation of celA, encoding a member of the family-5 of glycosyl hydrolases, abolished the endoglucanase activity in L. pneumophila culture supernatants. The cloned celA gene conferred activity upon recombinant Escherichia coli. Thus, CelA is the major secreted endoglucanase of L. pneumophila. Mutants inactivated for celA grew normally in protozoa and macrophage, indicating that CelA is not required for the intracellular phase of L. pneumophila. The CelA endoglucanase is one of at least 25 proteins secreted by the type II system of L. pneumophila and the 17th type of enzyme effector associated with this pathway. Only a subset of the other Legionella species tested expressed secreted endoglucanase activity, suggesting that the T2S output differs among the different legionellae. Overall, this study represents the first documentation of an endoglucanase (EC 3.2.1.4) being produced by a strain of Legionella.

Original languageEnglish (US)
Pages (from-to)256-264
Number of pages9
JournalFEMS Microbiology Letters
Volume300
Issue number2
DOIs
StatePublished - Nov 2009

Keywords

  • Cellulase
  • Endoglucanase
  • Intracellular infection
  • Legionella pneumophila
  • Type II protein secretion

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics

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