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Probing the Pal‐peptidoglycan interaction
Author(s) -
Ward Zachary,
Liu Xinbei,
Lewis Sean D,
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.631.46
Subject(s) - peptidoglycan , escherichia coli , lipid ii , microbiology and biotechnology , immune system , cell wall , biology , bacteria , bacterial cell structure , chemistry , biochemistry , genetics , gene
Sepsis can be caused by a bacterial infection in the human bloodstream, upon which the immune system is over‐activated causing hyper‐inflammation throughout the body. One of the molecules in Escherichia coli ( E. coli ) that is thought to contribute to the over‐exuberant immune response is peptidoglycan‐associated lipoprotein (PAL). PAL binds tightly to peptidoglycan in the E. coli cell, but has been shown to be released from E. coli under certain conditions. We propose that modulating the PAL‐peptidoglycan interaction would have an effect on E. coli 's ability to release PAL. Here, we describe an enzyme linked immunosorbent assay in which we measure and quantify changes to the PAL‐peptidoglycan interaction. Preliminary data suggest we were able to dramatically decrease binding of PAL to peptidoglycan with a single amino acid change in PAL. Support or Funding Information Rochester Institute of Technology This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .