Determination of the cell wall polysaccharide and teichoic acid structures from Lactococcus lactis IL1403

2018 ◽  
Vol 462 ◽  
pp. 39-44 ◽  
Author(s):  
Evgeny Vinogradov ◽  
Irina Sadovskaya ◽  
Pascal Courtin ◽  
Saulius Kulakauskas ◽  
Thierry Grard ◽  
...  
2014 ◽  
Vol 197 (2) ◽  
pp. 343-353 ◽  
Author(s):  
Megan Liszewski Zilla ◽  
Yvonne G. Y. Chan ◽  
Justin Mark Lunderberg ◽  
Olaf Schneewind ◽  
Dominique Missiakas

Bacillus anthracis, the causative agent of anthrax, replicates as chains of vegetative cells by regulating the separation of septal peptidoglycan. Surface (S)-layer proteins and associated proteins (BSLs) function as chain length determinants and bind to the secondary cell wall polysaccharide (SCWP). In this study, we identified theB. anthracislcpDmutant, which displays increased chain length and S-layer assembly defects due to diminished SCWP attachment to peptidoglycan. In contrast, theB. anthracislcpB3variant displayed reduced cell size and chain length, which could be attributed to increased deposition of BSLs. In other bacteria, LytR-CpsA-Psr (LCP) proteins attach wall teichoic acid (WTA) and polysaccharide capsule to peptidoglycan.B. anthracisdoes not synthesize these polymers, yet its genome encodes six LCP homologues, which, when expressed inS. aureus, promote WTA attachment. We propose a model wherebyB. anthracisLCPs promote attachment of SCWP precursors to discrete locations in the peptidoglycan, enabling BSL assembly and regulated separation of septal peptidoglycan.


2018 ◽  
Vol 461 ◽  
pp. 25-31 ◽  
Author(s):  
Evgeny Vinogradov ◽  
Irina Sadovskaya ◽  
Thierry Grard ◽  
James Murphy ◽  
Jennifer Mahony ◽  
...  

2021 ◽  
Vol 12 ◽  
Author(s):  
Héctor L. Villalobos-Duno ◽  
Laura A. Barreto ◽  
Álvaro Alvarez-Aular ◽  
Héctor M. Mora-Montes ◽  
Nancy E. Lozoya-Pérez ◽  
...  

Sporothrix schenckii, Sporothrix brasiliensis, and Sporothrix globosa are the main causative agents of sporotrichosis, a human subcutaneous mycosis. Differences in virulence patterns are associated with each species but remain largely uncharacterized. The S. schenckii and S. brasiliensis cell wall composition and virulence are influenced by the culturing media, with little or no influence on S. globosa. By keeping constant the culturing media, we compared the cell wall composition of three S. schenckii and two S. brasiliensis strains, previously described as presenting different virulence levels on a murine model of infection. The cell wall composition of the five Sporothrix spp. strains correlated with the biochemical composition of the cell wall previously reported for the species. However, the rhamnose-to-β-glucan ratio exhibits differences among strains, with an increase in cell wall rhamnose-to-β-glucan ratio as their virulence increased. This relationship can be expressed mathematically, which could be an important tool for the determination of virulence in Sporothrix spp. Also, structural differences in rhamnomannan were found, with longer side chains present in strains with lower virulence reported for both species here studied, adding insight to the importance of this polysaccharide in the pathogenic process of these fungi.


1971 ◽  
Vol 134 (3) ◽  
pp. 600-617 ◽  
Author(s):  
Gerald Schiffman ◽  
Donald L. Bornstein ◽  
Robert Austrian

Methods are described for the separation of the C or cell wall polysaccharide from the Cs or soluble C-like capsular polysaccharide of Cs pneumococcal strains. Immunologic analysis has shown that both the C and Cs polysaccharides of a variety of pneumococcal strains are heterogeneous and that the dissimilarities appear to reside in the mucopeptide portion of the molecule or in the region of its attachment to the teichoic acid moiety of the molecule rather than in the teichoic acid fraction. Differences of the type described have been observed in the C polysaccharides of wild-type capsulated strains of several types, in those of independently isolated noncapsulated variants derived from a single strain of a given capsular type, and in the C and Cs polysaccharides of spontaneous mutant or transformed strains of pneumococci producing capsules of Cs polysaccharide.


2003 ◽  
Vol 69 (6) ◽  
pp. 3377-3384 ◽  
Author(s):  
Jacques-Edouard Germond ◽  
Mich�le Delley ◽  
Christophe Gilbert ◽  
Dani�le Atlan

ABSTRACT Belonging to the subtilase family, the cell surface proteinase (CSP) PrtB of Lactobacillus delbrueckii subsp. bulgaricus differs from other CSPs synthesized by lactic acid bacteria. Expression of the prtB gene under its own promoter was shown to complement the proteinase-deficient strain MG1363 (PrtP− PrtM−) of Lactococcus lactis subsp. cremoris. Surprisingly, the maturation process of PrtB, unlike that of lactococcal CSP PrtPs, does not require a specific PrtM-like chaperone. The carboxy end of PrtB was previously shown to be different from the consensus anchoring region of other CSPs and exhibits an imperfect duplication of 59 amino acids with a high lysine content. By using a deletion strategy, the removal of the last 99 amino acids, including the degenerated anchoring signal (LPKKT), was found to be sufficient to release a part of the truncated PrtB into the culture medium and led to an increase in PrtB activity. This truncated PrtB is still active and enables L. lactis MG1363 to grow in milk supplemented with glucose. By contrast, deletion of the last 806 amino acids of PrtB led to the secretion of an inactive proteinase. Thus, the utmost carboxy end of PrtB is involved in attachment to the bacterial cell wall. Proteinase PrtB constitutes a powerful tool for cell surface display of heterologous proteins like antigens.


1994 ◽  
Vol 13 (3) ◽  
pp. 363-382 ◽  
Author(s):  
Marijke Gruter ◽  
Didier Billy ◽  
Pieter de Waard ◽  
Jan Kuiper ◽  
Johannis Kamerling ◽  
...  

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