Enteric YaiW is a surface-exposed outer membrane lipoprotein that affects sensitivity to an antimicrobial peptide

Markus F F Arnold, Paola Caro-Hernandez, Karen Tan, Giulia Runti, Silvia Wehmeier, Marco Scocchi, William T Doerrler, Graham C Walker, Gail P Ferguson

Research output: Contribution to journalArticlepeer-review


yaiW is a previously uncharacterized gene found in enteric bacteria that is of particular interest because it is located adjacent to the sbmA gene, whose bacA ortholog is required for Sinorhizobium meliloti symbiosis and Brucella abortus pathogenesis. We show that yaiW is cotranscribed with sbmA in Escherichia coli and Salmonella enterica serovar Typhi and Typhimurium strains. We present evidence that the YaiW is a palmitate-modified surface exposed outer membrane lipoprotein. Since BacA function affects the very-long-chain fatty acid (VLCFA) modification of S. meliloti and B. abortus lipid A, we tested whether SbmA function might affect either the fatty acid modification of the YaiW lipoprotein or the fatty acid modification of enteric lipid A but found that it did not. Interestingly, we did observe that E. coli SbmA suppresses deficiencies in the VLCFA modification of the lipopolysaccharide of an S. meliloti bacA mutant despite the absence of VLCFA in E. coli. Finally, we found that both YaiW and SbmA positively affect the uptake of proline-rich Bac7 peptides, suggesting a possible connection between their cellular functions.

Original languageEnglish
Pages (from-to)436-44
Number of pages9
JournalJournal of Bacteriology
Issue number2
Publication statusPublished - Jan 2014


  • Antimicrobial Cationic Peptides
  • Bacterial Outer Membrane Proteins
  • Brucella abortus
  • Escherichia coli
  • Escherichia coli Proteins
  • Genes, Suppressor
  • Lipoproteins
  • Microbial Sensitivity Tests
  • Salmonella typhimurium
  • Sinorhizobium meliloti
  • Transcription, Genetic
  • Transferases


Dive into the research topics of 'Enteric YaiW is a surface-exposed outer membrane lipoprotein that affects sensitivity to an antimicrobial peptide'. Together they form a unique fingerprint.

Cite this