The structure of PilA from Acinetobacter baumannii AB5075 suggests a mechanism for functional specialization in Acinetobacter type IV pili

Leslie A. Ronish, Erik Lillehoj, James K. Fields, Eric J. Sundberg, Kurt H Piepenbrink

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Type IV pili (T4P) are bacterial appendages composed of protein subunits, called pilins, noncovalently assembled into helical fibers. T4P are essential, in many bacterial species, for processes as diverse as twitching motility, natural competence, biofilm or microcolony formation, and host cell adhesion. The genes encoding type IV pili are found universally in the Gram-negative, aerobic, nonflagellated, and pathogenic coccobacillus Acinetobacter baumannii, but there is considerable variation in PilA, the major protein subunit, both in amino acid sequence and in glycosylation patterns. Here we report the X-ray crystal structure of PilA from AB5075, a recently characterized, highly virulent isolate, at 1.9 Å resolution and compare it to homologues from A. baumannii strains ACICU and BIDMC57, which are C-terminally glycosylated. These structural comparisons revealed that PilAAB5075 exhibits a distinctly electronegative surface chemistry. To understand the functional consequences of this change in surface electrostatics, we complemented a pilA knockout strain with divergent pilA genes from ACICU, BIDMC57, and AB5075. The resulting transgenic strains showed differential twitching motility and biofilm formation while maintaining the ability to adhere to epithelial cells. PilAAB5075 and PilAACICU, although structurally similar, promote different characteristics, favoring twitching motility and biofilm formation, respectively. These results support a model in which differences in pilus electrostatics affect the equilibrium of microcolony formation, which in turn alters the balance between motility and biofilm formation in Acinetobacter.

Original languageEnglish (US)
Pages (from-to)218-230
Number of pages13
JournalJournal of Biological Chemistry
Volume294
Issue number1
DOIs
StatePublished - Jan 1 2019

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Acinetobacter baumannii
Acinetobacter
Biofilms
Protein Subunits
Static Electricity
Electrostatics
Bacterial Fimbriae
Bacterial Physiological Phenomena
Fimbriae Proteins
Glycosylation
Gene encoding
Aptitude
Cell adhesion
Surface chemistry
Cell Adhesion
Mental Competency
Genes
Amino Acid Sequence
Crystal structure
Epithelial Cells

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

The structure of PilA from Acinetobacter baumannii AB5075 suggests a mechanism for functional specialization in Acinetobacter type IV pili. / Ronish, Leslie A.; Lillehoj, Erik; Fields, James K.; Sundberg, Eric J.; Piepenbrink, Kurt H.

In: Journal of Biological Chemistry, Vol. 294, No. 1, 01.01.2019, p. 218-230.

Research output: Contribution to journalArticle

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