Artigo Acesso aberto Revisado por pares

Characterizing of the Effects of Pal‐Peptidoglycan Interaction

2020; Wiley; Volume: 34; Issue: S1 Linguagem: Inglês

10.1096/fasebj.2020.34.s1.01895

ISSN

1530-6860

Autores

Xinbei Liu, Sean D Lewis, Zack Ward, Lea Michel,

Tópico(s)

Genomics and Phylogenetic Studies

Resumo

Peptidoglycan‐associated lipoprotein, Pal, is found in the outer membrane of Escherichia coli (E. coli) and other Gram‐negative bacteria. Previous research has shown that under certain conditions, including several animal models of sepsis, Pal is released from E. coli and is thought to be implicated in the clinical condition of sepsis. In Gram‐negative bacteria, Pal is non‐covalently, but tightly bound to peptidoglycan. We hypothesize that the strong Pal‐peptidoglycan interactions influence Pal’s ability to be released from E. coli. Site‐directed mutants of E. coli Pal have been prepared and studied to determine how Pal’s altered binding affinities to peptidoglycan affect Pal’s release from E. coli. Preliminary results suggest that other factors, in addition to the Pal‐peptidoglycan interaction, are responsible for Pal’s release from E. coli .

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