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ABI domain‐containing proteins contribute to surface protein display and cell division in Staphylococcus aureus
Author(s) -
Frankel Matthew B.,
Wojcik Brandon M.,
DeDent Andrea C.,
Missiakas Dominique M.,
Schneewind Olaf
Publication year - 2010
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2010.07334.x
Subject(s) - biology , cell envelope , signal peptide , mutant , cell division , transmembrane protein , microbiology and biotechnology , peptidoglycan , transposon mutagenesis , membrane protein , transmembrane domain , gene , genetics , cell , transposable element , peptide sequence , escherichia coli , receptor , membrane
Summary The human pathogen Staphyloccocus aureus requires cell wall anchored surface proteins to cause disease. During cell division, surface proteins with YSIRK signal peptides are secreted into the cross‐wall, a layer of newly synthesized peptidoglycan between separating daughter cells. The molecular determinants for the trafficking of surface proteins are, however, still unknown. We screened mutants with non‐redundant transposon insertions by fluorescence‐activated cell sorting for reduced deposition of protein A (SpA) into the staphylococcal envelope. Three mutants, each of which harboured transposon insertions in genes for transmembrane proteins, displayed greatly reduced envelope abundance of SpA and surface proteins with YSIRK signal peptides. Characterization of the corresponding mutations identified three transmembrane proteins with abortive infectivity (ABI) domains, elements first described in lactococci for their role in phage exclusion. Mutations in genes for ABI domain proteins, designated spdA , spdB and spdC ( s urface p rotein d isplay), diminish the expression of surface proteins with YSIRK signal peptides, but not of precursor proteins with conventional signal peptides. spdA , spdB and spdC mutants display an increase in the thickness of cross‐walls and in the relative abundance of staphylococci with cross‐walls, suggesting that spd mutations may represent a possible link between staphylococcal cell division and protein secretion.