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IN
Journal article
Anchorless cell surface proteins function as laminin-binding adhesins inLactobacillus rhamnosus FSMM22
Ni Putu Desy Aryantini Daisuke Kondoh Keita Nishiyama Yuj i Yamamoto Takao Mukai I NENGAH SUJAYA Tadasu Urashima Kenji Fukuda
Volume : 364 Nomor : 6 Published : 2017, March
FEMS Microbiology Letters
Abstrak
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