Anchorless cell surface proteins function as laminin-binding adhesins in Lactobacillus rhamnosus FSMM22

Ni Putu Desy Aryantini, Daisuke Kondoh, Keita Nishiyama, Yuji Yamamoto, Takao Mukai, I. Nengah Sujaya, Tadasu Urashima, Kenji Fukuda

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Anchorless cell surface proteins (CSPs) were extracted with 1 M lithium chloride solution from Lactobacillus rhamnosus FSMM22. Loss of the anchorless CSPs resulted in a 2-fold decrease in FSMM22 cells bound to a constitutive extracellular matrix glycoprotein, laminin, in vitro. DNA-binding protein HU, glyceraldehyde-3-phosphate dehydrogenase, lactate dehydrogenase and 30S ribosomal protein S19 (RpsS) were identified by mass spectrometry in the extract as laminin-binding adhesins. Among the four proteins, RpsS was immunohistochemically confirmed to exist on the cell surface. Our findings strongly suggest that anchorless CSPs can enhance bacterial adhesion to the host.

Original languageEnglish
Article numberfnx056
JournalFEMS microbiology letters
Volume364
Issue number6
DOIs
Publication statusPublished - 2017 Mar 1
Externally publishedYes

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Keywords

  • Cell surface proteins
  • Host-microbial interactions
  • Lactic acid bacteria
  • Laminin
  • Probiotics
  • Ribosomal proteins

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics

Cite this

Aryantini, N. P. D., Kondoh, D., Nishiyama, K., Yamamoto, Y., Mukai, T., Sujaya, I. N., Urashima, T., & Fukuda, K. (2017). Anchorless cell surface proteins function as laminin-binding adhesins in Lactobacillus rhamnosus FSMM22. FEMS microbiology letters, 364(6), [fnx056]. https://doi.org/10.1093/femsle/fnx056