Identification of collagen-binding proteins in Lactobacillus spp. with surface-enhanced laser desorption/ionization-time of flight ProteinChip technology.
Biosurfactants produced by Lactobacillus fermentum RC-14, L. rhamnosus GR-1 and 36, and L. casei Shirota were found to contain proteins that bind to both collagen types III and VI, as determined by surface-enhanced laser desorption/ionization (SELDI)-time of flight mass spectrometry. Both collagen types III and VI immobilized on SELDI preactivated ProteinChip arrays detected several different sizes (2 to 48 kDa) of collagen-binding proteins. Overall, the RC-14-produced biosurfactant contained the greatest number of collagen-binding proteins (RC-14 > GR-1 > 36 > Shirota), including the mature form of a previously cloned 29-kDa collagen-binding protein (referred to in its mature 26-kDa form). Although biosurfactants isolated from L. casei Shirota and L. rhamnosus 36 and GR-1 also contain several collagen-binding proteins, they do not contain the 26-kDa collagen-binding protein. Together, these results demonstrate the utility of the SELDI system as a means of rapidly characterizing clinically important but complex biosurfactant solutions.
Howard
J C
JC
Hand and Upper Limb Centre, London, Ontario, Canada.
Heinemann
C
C
Thatcher
B J
BJ
Martin
B
B
Gan
B S
BS
Reid
G
G
D002352:Carrier Proteins / Q000032:analysis* / Q000378:metabolism; D003094:Collagen / Q000378:metabolism*; D016023:Integrins / Q000032:analysis* / Q000378:metabolism; D007778:Lactobacillus / Q000145:classification / Q000302:isolation & purification / Q000502:physiology*; D007780:Lacticaseibacillus casei / Q000502:physiology; D019151:Peptide Library; D038981:Receptors, Collagen; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D002352:Carrier Proteins; D016023:Integrins; D019151:Peptide Library; D038981:Receptors, Collagen; D003094:Collagen