An Acid Up-Regulated Surface Protein of Lactobacillus paracasei Strain GCRL 46 is Phylogenetically Related to the Secreted Glucan- (GpbB) and Immunoglobulin-Binding (SibA) Protein of Pathogenic Streptococci

Autor: Susan J Pepper, Margaret L. Britz
Jazyk: angličtina
Rok vydání: 2019
Předmět:
0301 basic medicine
Autolysis (biology)
Lactobacillus casei
Lactobacillus paracasei
030106 microbiology
Catalysis
Bacterial cell structure
Article
lcsh:Chemistry
Inorganic Chemistry
03 medical and health sciences
chemistry.chemical_compound
Bacterial Proteins
Physical and Theoretical Chemistry
lcsh:QH301-705.5
Molecular Biology
Spectroscopy
Phylogeny
Peptidoglycan turnover
biology
Streptococcus
Chemistry
Organic Chemistry
SibA
General Medicine
Lacticaseibacillus paracasei
Hydrogen-Ion Concentration
biology.organism_classification
CHAP
Computer Science Applications
cell-wall hydrolase
030104 developmental biology
lcsh:Biology (General)
lcsh:QD1-999
Biochemistry
Antigens
Surface
Electrophoresis
Polyacrylamide Gel
Peptidoglycan
Bifidobacterium
acid resistance
PcsB
Immunoglobulin binding
Enterococcus
Cysteine
Zdroj: International Journal of Molecular Sciences
Volume 20
Issue 7
International Journal of Molecular Sciences, Vol 20, Iss 7, p 1610 (2019)
ISSN: 1422-0067
Popis: Bacterial cell wall hydrolases, including amidases and peptidases, play a critical role in peptidoglycan turnover during growth, impacting daughter cell separation, and cell death, through autolysis. When exploring the regulation of protein expression across the growth cycle of an acid-resistant strain of Lactobacillus paracasei, GCRL 46, we observed temporal up-regulation of proteins in the 40&ndash
45 kDa molecular weight range for whole-cell extracts when culturing in fermenters at a controlled pH of 4.0 versus optimum growth pH of 6.3. Up-regulation of proteins in this size range was not detected in SDS-PAGE gels of the cytosolic fraction, but was routinely detected following growth at low pH in whole cells and cell debris obtained after bead beating and centrifugation, indicating a cell surface location. N-terminal sequencing and in silico analyses showed sequence similarity with proteins in the L. casei group (L. casei, L. paracasei and L. rhamnosus) which were variously annotated as uncharacterized proteins, surface antigens, possible TrsG proteins, CHAP (cysteine, histidine-dependent amidohydrolases/peptidases)-domain proteins or putative peptidoglycan d,l-endopeptidase due to the presence of a CwlO domain. This protein is a homologue of the p40 (Msp2) secreted protein of L. rhamnosus LGG, which is linked to probiotic functionality in this species, and is phylogenetically related to structurally-similar proteins found in Enterococcus, Streptococcus and Bifidobacterium species, including the glucan-binding (GbpB), surface antigen (SagA) proteins detected in pathogenic group A streptococci species as secreted, immunoglobulin-binding (SibA) proteins (also named PcsB). Three-dimensional (3D) modelling predicted structural similarities in the CHAP proteins from the L. casei group and streptococcal species, indicating retention of overall architecture despite sequence divergence, and an implied retention of function during evolution. A phylogenetically-related hydrolase also contained the CwlO domain with a NLPC_P60 domain, and showed similar overall but distinct architecture to the CHAP proteins. We concluded that the surface-located, CHAP protein in L. casei is up-regulated during long-term exposure to acidic conditions during growth but not during acid shock.
Databáze: OpenAIRE
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