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Probing the Effect of the Pal‐Peptidoglycan Interaction on Pal Release from Escherichia coli
Author(s) -
Liu Xinbei,
Lewis Sean D,
Ward Zachary,
LaClair Ciara,
Michel Lea Vacca
Publication year - 2019
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2019.33.1_supplement.631.27
Subject(s) - peptidoglycan , escherichia coli , lipid ii , microbiology and biotechnology , mutant , biology , chemistry , biochemistry , cell wall , gene
Peptidoglycan‐associated lipoprotein, Pal, is inserted into the outer membrane of Escherichia coli ( E. coli ) and other Gram‐negative bacteria. Under certain conditions, including several animal models of sepsis, Pal is released from E. coli and is thought to be involved in the clinical condition of sepsis. As its name infers, Pal is tethered to the peptidoglycan layer. We propose that the strong noncovalent Pal‐peptidoglycan interaction may have an effect on Pal's ability to be released from E. coli . We tested several site‐directed mutants of Pal with altered affinities to peptidoglycan to determine the effect of those mutations on Pal's release from E. coli . Preliminary results suggest the Pal‐peptidoglycan interaction, alone, does not dictate its release from E. coli . Support or Funding Information Rochester Institute of Technology; The Rochester Institute of Technology Research Initiative for Scientific Enhancement (RIT‐RISE) This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .

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