title: Structural Diversity in the Type IV Pili of Multidrug-resistant Acinetobacter.
abstract: Acinetobacter baumannii is a Gram-negative coccobacillus found primarily in hospital settings that has recently emerged as a source of hospital-acquired infections. A. baumannii expresses a variety of virulence factors, including type IV pili, bacterial extracellular appendages often essential for attachment to host cells. Here, we report the high resolution structures of the major pilin subunit, PilA, from three Acinetobacter strains, demonstrating that A. baumannii subsets produce morphologically distinct type IV pilin glycoproteins. We examine the consequences of this heterogeneity for protein folding and assembly as well as host-cell adhesion by Acinetobacter Comparisons of genomic and structural data with pilin proteins from other species of soil gammaproteobacteria suggest that these structural differences stem from evolutionary pressure that has resulted in three distinct classes of type IVa pilins, each found in multiple species.
authors.affiliation: From the Institute of Human Virology and.
authors.forename: Kurt H
authors.initials: KH
authors.lastname: Piepenbrink
authors.affiliation: Pediatrics, and.
authors.forename: Erik
authors.initials: E
authors.lastname: Lillehoj
authors.affiliation: Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, Missouri 63110.
authors.forename: Christian M
authors.initials: CM
authors.lastname: Harding
authors.affiliation: Department of Chemical and Biomolecular Engineering, Whiting School of Engineering, The Johns Hopkins University, Baltimore, Maryland 21218.
authors.forename: Jason W
authors.initials: JW
authors.lastname: Labonte
authors.affiliation: Department of Chemical and Biomolecular Engineering, Whiting School of Engineering, The Johns Hopkins University, Baltimore, Maryland 21218.
authors.forename: Xiaotong
authors.initials: X
authors.lastname: Zuo
authors.affiliation: From the Institute of Human Virology and.
authors.forename: Chelsea A
authors.initials: CA
authors.lastname: Rapp
authors.affiliation: The Center for Microbial Pathogenesis in the Research Institute at Nationwide Children's Hospital and Department of Pediatrics, The Ohio State University College of Medicine, Columbus, Ohio 43205, and.
authors.forename: Robert S
authors.initials: RS
authors.lastname: Munson
authors.affiliation: Departments of Medicine.|Baltimore Veterans Affairs Medical Center, Baltimore, Maryland 21201.|Pathology, University of Maryland School of Medicine, Baltimore, Maryland 21201.
authors.forename: Simeon E
authors.initials: SE
authors.lastname: Goldblum
authors.affiliation: Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, Missouri 63110.
authors.forename: Mario F
authors.initials: MF
authors.lastname: Feldman
authors.affiliation: Department of Chemical and Biomolecular Engineering, Whiting School of Engineering, The Johns Hopkins University, Baltimore, Maryland 21218.
authors.forename: Jeffrey J
authors.initials: JJ
authors.lastname: Gray
authors.affiliation: From the Institute of Human Virology and esundberg@ihv.umaryland.edu.|Departments of Medicine.|Microbiology and Immunology.
authors.forename: Eric J
authors.initials: EJ
authors.lastname: Sundberg
mesh_terms: D000151:Acinetobacter Infections / Q000382:microbiology; D040981:Acinetobacter baumannii / Q000737:chemistry / Q000145:classification / Q000187:drug effects* / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D024901:Drug Resistance, Multiple, Bacterial; D019143:Evolution, Molecular; D010861:Fimbriae, Bacterial / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D020563:Gammaproteobacteria / Q000737:chemistry / Q000145:classification / Q000302:isolation & purification / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D006801:Humans; D008958:Models, Molecular; D010802:Phylogeny; D012988:Soil Microbiology
chemical_list: D001426:Bacterial Proteins
keywords: cell adhesion; glycosylation; microbial pathogenesis; protein folding; type IV pili; x-ray crystallography