title: Modeling Diversity in Structures of Bacterial Outer Membrane Lipids.
abstract: Lipopolysaccharides (LPSs) are vital components of the outer membrane of Gram-negative bacteria, and they act as extremely strong stimulators of innate immunity in diverse eukaryotic species. The primary immunostimulatory center of the LPS molecule is lipid A, a disaccharide-bound lipophilic domain. Considering the broad diversity in bacterial species, there are variations in the lipid A structures and their immunogenic potencies. In this work, we model the lipid A structures of eight commensal or human pathogenic bacterial species: Helicobacter pylori, Porphyromonas gingivalis, Bacteroides fragilis, Bordetella pertussis, Chlamydia trachomatis, Campylobacter jejuni, Neisseria meningitidis, and Salmonella minnesota. The membrane properties of these bacterial species were characterized and compared using molecular simulations. The structure-property relationships that emerge from this lipid A molecular library highlight the roles of acyl chain lengths, number of chains, phosphorylation state, membrane composition, and counterion charge in regulating the phase transition temperature of the membrane, diffusion coefficient of the lipids, and membrane thickness. The molecular and structural insights provided reveal the diversity in bacterial outer membrane lipids and their contribution to human disease and immunity.
authors.affiliation: Department of Biomedical and Chemical Engineering, Syracuse University , Syracuse, New York 13244, United States.
authors.forename: Huilin
authors.initials: H
authors.lastname: Ma
authors.affiliation: Department of Biomedical and Chemical Engineering, Syracuse University , Syracuse, New York 13244, United States.
authors.forename: Daniel D
authors.initials: DD
authors.lastname: Cummins
authors.affiliation: Department of Biomedical and Chemical Engineering, Syracuse University , Syracuse, New York 13244, United States.
authors.forename: Natalie Brooke
authors.initials: NB
authors.lastname: Edelstein
authors.affiliation: Department of Biomedical and Chemical Engineering, Syracuse University , Syracuse, New York 13244, United States.
authors.forename: Jerry
authors.initials: J
authors.lastname: Gomez
authors.affiliation: Department of Biomedical and Chemical Engineering, Syracuse University , Syracuse, New York 13244, United States.
authors.forename: Aliza
authors.initials: A
authors.lastname: Khan
authors.affiliation: Department of Biomedical and Chemical Engineering, Syracuse University , Syracuse, New York 13244, United States.
authors.forename: Masud Dikita
authors.initials: MD
authors.lastname: Llewellyn
authors.affiliation: Department of Biomedical and Chemical Engineering, Syracuse University , Syracuse, New York 13244, United States.
authors.forename: Tara
authors.initials: T
authors.lastname: Picudella
authors.affiliation: Department of Biomedical and Chemical Engineering, Syracuse University , Syracuse, New York 13244, United States.
authors.forename: Sarah Rose
authors.initials: SR
authors.lastname: Willsey
authors.affiliation: Department of Biomedical and Chemical Engineering, Syracuse University , Syracuse, New York 13244, United States.
authors.forename: Shikha
authors.identifier: http://orcid.org/0000-0003-1170-8461
authors.initials: S
authors.lastname: Nangia
mesh_terms: D001419:Bacteria / Q000166:cytology*; D002462:Cell Membrane / Q000737:chemistry*; D008563:Membrane Lipids / Q000737:chemistry*; D008958:Models, Molecular; D008968:Molecular Conformation; D013045:Species Specificity; D044366:Transition Temperature
chemical_list: D008563:Membrane Lipids