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Investigating Pal's Interaction with Peptidoglycan
Author(s) -
Lewis Sean D,
Liu Xinbei,
Ward Zack,
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.631.25
Subject(s) - peptidoglycan , periplasmic space , escherichia coli , mutagenesis , biology , biochemistry , microbiology and biotechnology , chemistry , cell wall , mutant , gene
Peptidoglycan associated lipoprotein (Pal) has been shown to exhibit a unique dual orientation in Escherichia coli ( E. coli ). That is, Pal has two subpopulations, one surface exposed subpopulation and one periplasmic subpopulation. The periplasmic Pal subpopulation binds tightly (but noncovalently) to peptidoglycan. Both subpopulations of Pal are thought to be released from E. coli under certain conditions, and released Pal has been shown to be implicated in the clinical condition of sepsis. This study uses site‐directed mutagenesis and ultracentrifugation to elucidate the detailed structural interaction between Pal and peptidoglycan, with the long‐term goal of understanding the role of that interaction in Pal's release from E. coli . Preliminary data suggest several key residues in Pal dictate the Pal‐peptidoglycan interaction. Support or Funding Information Rochester Institute of Technology, College of Science This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .