The thin pili of Acinetobacter sp. strain BD413 mediate adhesion to biotic and abiotic surfaces.
Two structurally different appendages, thin and thick pili, are found in members of the genus Acinetobacter. The presence of pilus structures correlates with different phenotypes, such as adherence to surfaces, a trait not only observed in pathogenic Acinetobacter species, as well as motility. However, their distinct individual roles were unknown. To characterize the role of different pili in the physiology of Acinetobacter, we isolated the thin pili from the cell surface of Acinetobacter sp. strain BD413 (recently recognized as representative of Acinetobacter baylyi), a soil bacterium that rapidly takes up naked DNA from its environment. Electron microscopy revealed that the pilus has an external diameter of 2 to 3 nm for single filaments. The filaments are packed into right-handed bundles. The major protein constituting the pilus was purified, and the encoding gene, acuA, was cloned. AcuA was found to be weakly related to the structural subunit of F17 pili of Escherichia coli. Analyses of the acuA flanking DNA region led to the identification of three closely associated genes, acuD, acuC, and acuG, whose deduced proteins are similar to chaperone, usher, and adhesin of F17-related pili, respectively. Transcriptional analyses revealed that acuA expression is maximal in the late-stationary-growth phase. Mutation of acuA led to a loss of thin pili and concomitantly loss of adhesion to polystyrene and erythrocytes but not loss of competence. Therefore, thin pili of Acinetobacter sp. strain BD413 are suggested to be assembled by the chaperone/usher pathway and are involved in adherence to biotic and abiotic surfaces.
Gohl
Olivia
O
Institute of Microbiology and Genetics, Georg-August-Universität, Göttingen, Germany.
Friedrich
Alexandra
A
Hoppert
Michael
M
Averhoff
Beate
B
D000150:Acinetobacter / Q000235:genetics / Q000502:physiology* / Q000648:ultrastructure; D000595:Amino Acid Sequence; D001422:Bacterial Adhesion / Q000502:physiology*; D001426:Bacterial Proteins / Q000235:genetics / Q000502:physiology; D001483:Base Sequence; D004269:DNA, Bacterial / Q000235:genetics; D004912:Erythrocytes / Q000382:microbiology; D004926:Escherichia coli / Q000235:genetics; D010861:Fimbriae, Bacterial / Q000235:genetics / Q000502:physiology* / Q000648:ultrastructure; D015964:Gene Expression Regulation, Bacterial; D005798:Genes, Bacterial; D005816:Genetic Complementation Test; D006801:Humans; D007091:Image Processing, Computer-Assisted; D066298:In Vitro Techniques; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D005810:Multigene Family; D009154:Mutation; D011137:Polystyrenes; D017386:Sequence Homology, Amino Acid; D013499:Surface Properties
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D011137:Polystyrenes