TY - JOUR
T1 - Structural diversity in the type IV Pili of multidrug-resistant acinetobacter
AU - Piepenbrink, Kurt H.
AU - Lillehoj, Erik
AU - Harding, Christian M.
AU - Labonte, Jason W.
AU - Zuo, Xiaotong
AU - Rapp, Chelsea A.
AU - Munson, Robert S.
AU - Goldblum, Simeon E.
AU - Feldman, Mario F.
AU - Gray, Jeffrey J.
AU - Sundberg, Eric J.
N1 - Funding Information:
This work was supported in part by National Institutes of Health Grant R01 AI114902 (to E. J. S.). The authors declare that they have no conflicts of interest with the contents of this article. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health. Supported by National Institutes of Health Training Grant T32 AI095190 and National Institutes of Health Fellowship F32 AI110045. Supported by National Institutes of Health Fellowship F32 CA189246. Acknowledgments-We thank the staff at Argonne National Laboratory Advanced Photon Source, General Medical Sciences and Cancer Institutes Structural Biology Facility, beam lines 23ID-D and 23ID-B, and the staff at Stanford Synchrotron Radiation Lightsource, beam line 12-2, for technical assistance with x-ray data collection. We also thank Dr. Angela Wilks for the use of the circular dichroism spectrophotometer.
PY - 2016/10/28
Y1 - 2016/10/28
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84994031770&partnerID=8YFLogxK
U2 - 10.1074/jbc.M116.751099
DO - 10.1074/jbc.M116.751099
M3 - Article
C2 - 27634041
AN - SCOPUS:84994031770
SN - 0021-9258
VL - 291
SP - 22924
EP - 22935
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 44
ER -