Anchorless cell surface proteins function as laminin-binding adhesins in Lactobacillus rhamnosus FSMM22. Issue 6 (9th March 2017)

• Record Type: Journal Article
• Authors: Aryantini, Ni Putu Desy; Kondoh, Daisuke; Nishiyama, Keita; Yamamoto, Yuji; Mukai, Takao; Sujaya, I Nengah; Urashima, Tadasu; Fukuda, Kenji
• Is Part Of: FEMS microbiology letters. Volume 364:Issue 6(2017)
• Publication Date: 2017-03-09
• Subjects: cell surface proteins -- host–microbial interactions -- lactic acid bacteria -- laminin -- probiotics -- ribosomal proteins; Microbiology -- Periodicals; 579
• DOI: 10.1093/femsle/fnx056
• Languages: English
• ISSNs: 0378-1097

Abstract

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. Abstract : Laminin-binding cell surface proteins in Lactobacillus rhamnosus FSMM22.