MalE of group A Streptococcus participates in the rapid transport of maltotriose and longer maltodextrins

Samuel Shelburne, Han Fang, Nnaja Okorafor, Paul Sumby, Izabela Sitkiewicz, David Keith, Payal Patel, Celest Austin, Edward A. Graviss, James M. Musser, Dar Chone Chow

Research output: Contribution to journalArticle

21 Scopus citations

Abstract

Study of the maltose/maltodextrin binding protein MalE in Escherichia coli has resulted in fundamental insights into the molecular mechanisms of microbial transport. Whether gram-positive bacteria employ a similar pathway for maltodextrin transport is unclear. The maltodextrin binding protein MalE has previously been shown to be key to the ability of group A Streptococcus (GAS) to colonize the oropharynx, the major site of GAS infection in humans. Here we used a multifaceted approach to elucidate the function and binding characteristics of GAS MalE. We found that GAS MalE is a central part of a highly efficient maltodextrin transport system capable of transporting linear maltodextrins that are up to at least seven glucose molecules long. Of the carbohydrates tested, GAS MalE had the highest affinity for maltotriose, a major breakdown product of starch in the human oropharynx. The thermodynamics and fluorescence changes induced by GAS MalE-maltodextrin binding were essentially opposite those reported for E. coli MaIE. Moreover, unlike E. coli MalE, GAS MalE exhibited no specific binding of maltose or cyclic maltodextrins. Our data show that GAS developed a transport system optimized for linear maltodextrins longer than two glucose molecules that has several key differences from its well-studied E. coli counterpart.

Original languageEnglish (US)
Pages (from-to)2610-2617
Number of pages8
JournalJournal of bacteriology
Volume189
Issue number7
DOIs
StatePublished - Apr 2007

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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