Variation and association of fibronectin-binding protein genes fnbA and fnbB in Staphylococcus aureus Japanese isolates

Miyo Murai, Hideaki Moriyama, Eiji Hata, Fumihiko Takeuchi, Junko Amemura-Maekawa

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Fibronectin-binding proteins A and B (FnBPA and FnBPB) mediate adhesion of Staphylococcus aureus to fibrinogen, elastin and fibronectin. FnBPA and FnBPB are encoded by two closely linked genes, fnbA and fnbB, respectively. With the exception of the N-terminal regions, the amino acid sequences of FnBPA and FnBPB are highly conserved. To investigate the genetics and evolution of fnbA and fnbB, the most variable regions, which code for the 67th amino acids of the A through B regions (A67-B) of fnbA and fnbB, were focused upon. Eighty isolates of S. aureus in Japan were sequenced and 19 and 18 types in fnbA and fnbB, respectively, identified. Although the phylogeny of fnbA and fnbB were found to be quite different, each fnbA type connected with a specific fnbB type, indicating that fnbA and fnbB mutate independently, whereas the combination of both genes after recombination is stable. Hence those fnbA-fnbB combinations were defined as FnBP sequence types (FnSTs). Representative isolates of each FnST were assigned distinct STs by multilocus sequence typing, suggesting correspondence of FnST with genome lineage. Linkage disequilibrium (LD) analysis of the A67-B region revealed that subdomains N2, N3 and FnBR1 form a LD block in fnbA, whereas N2 and N3 form two independent LD blocks in fnbB. N2-N3 three-dimensional structural models indicated that not only the variable amino acid residues, but also well-conserved amino acid residues between FnBPA and FnBPB, are located on the surface of the protein. These results highlight a molecular process of the FnBP that has evolved by mingled mutation and recombination with retention of functions.

Original languageEnglish (US)
Pages (from-to)312-325
Number of pages14
JournalMicrobiology and Immunology
Volume60
Issue number5
DOIs
StatePublished - May 1 2016

Fingerprint

Linkage Disequilibrium
Fibronectins
Staphylococcus aureus
Carrier Proteins
Amino Acids
Genetic Recombination
Genes
Multilocus Sequence Typing
Molecular Evolution
Elastin
Structural Models
Phylogeny
Fibrinogen
Amino Acid Sequence
Japan
Membrane Proteins
Genome
Mutation
bacterial fibronectin-binding proteins

Keywords

  • Fibronectin-binding protein
  • Linkage disequilibrium
  • Multilocus sequence typing
  • Staphylococcal aureus

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Virology

Cite this

Variation and association of fibronectin-binding protein genes fnbA and fnbB in Staphylococcus aureus Japanese isolates. / Murai, Miyo; Moriyama, Hideaki; Hata, Eiji; Takeuchi, Fumihiko; Amemura-Maekawa, Junko.

In: Microbiology and Immunology, Vol. 60, No. 5, 01.05.2016, p. 312-325.

Research output: Contribution to journalArticle

Murai, Miyo ; Moriyama, Hideaki ; Hata, Eiji ; Takeuchi, Fumihiko ; Amemura-Maekawa, Junko. / Variation and association of fibronectin-binding protein genes fnbA and fnbB in Staphylococcus aureus Japanese isolates. In: Microbiology and Immunology. 2016 ; Vol. 60, No. 5. pp. 312-325.
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AB - Fibronectin-binding proteins A and B (FnBPA and FnBPB) mediate adhesion of Staphylococcus aureus to fibrinogen, elastin and fibronectin. FnBPA and FnBPB are encoded by two closely linked genes, fnbA and fnbB, respectively. With the exception of the N-terminal regions, the amino acid sequences of FnBPA and FnBPB are highly conserved. To investigate the genetics and evolution of fnbA and fnbB, the most variable regions, which code for the 67th amino acids of the A through B regions (A67-B) of fnbA and fnbB, were focused upon. Eighty isolates of S. aureus in Japan were sequenced and 19 and 18 types in fnbA and fnbB, respectively, identified. Although the phylogeny of fnbA and fnbB were found to be quite different, each fnbA type connected with a specific fnbB type, indicating that fnbA and fnbB mutate independently, whereas the combination of both genes after recombination is stable. Hence those fnbA-fnbB combinations were defined as FnBP sequence types (FnSTs). Representative isolates of each FnST were assigned distinct STs by multilocus sequence typing, suggesting correspondence of FnST with genome lineage. Linkage disequilibrium (LD) analysis of the A67-B region revealed that subdomains N2, N3 and FnBR1 form a LD block in fnbA, whereas N2 and N3 form two independent LD blocks in fnbB. N2-N3 three-dimensional structural models indicated that not only the variable amino acid residues, but also well-conserved amino acid residues between FnBPA and FnBPB, are located on the surface of the protein. These results highlight a molecular process of the FnBP that has evolved by mingled mutation and recombination with retention of functions.

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