Structure of Pneumococcal Peptidoglycan Hydrolase LytB Reveals Insights into the Bacterial Cell Wall Remodeling and Pathogenesis

Bai, Xiaohui; Chen, Huijie; Jiang, Yong-Liang; Wen, Zhensong; Huang, Yubin; Wang, Cheng; Li, Qiong; Qi, Lei; Zhang, Jing-Ren; Chen, Yuxing; Zhou, Cong‐Zhao

doi:10.1074/jbc.m114.579714

Cited by 51 publications

(69 citation statements)

References 62 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The N ‐acetylglucosaminidase LytB (SPD_0853; p I of the mature protein 5.0), which is responsible for daughter cell separation (De las Rivas et al ., ), is also involved in pneumococcal attachment to nasopharyngeal cells, and in adhesion to and invasion of lung epithelial cells (Ramos‐Sevillano et al ., ; Bai et al ., ). LytB is also required for optimal in vitro biofilm formation (Moscoso et al ., ), and the addition of up to 0.5 μg ml −1 of purified LytB boosted biofilm formation by a lytB pneumococcal mutant (Domenech et al ., ).…”

Section: Resultsmentioning

confidence: 99%

“…PK, the binding mixture was digested with proteinase K (100 μg ml −1 ; 15 min, 37°C) after allowing the formation of the CbpF−DNA complex. (Ramos-Sevillano et al, 2011;Bai et al, 2014). LytB is also required for optimal in vitro biofilm formation (Moscoso et al, 2006), and the addition of up to 0.5 μg ml −1 of purified LytB boosted biofilm formation by a lytB pneumococcal mutant (Domenech et al, 2013a).…”

Section: Optimal Conditions For Cbp-dna Complex Formation In Vitromentioning

confidence: 99%

See 1 more Smart Citation

In vitro biofilm development of Streptococcus pneumoniae and formation of choline‐binding protein–DNA complexes

Domenech

Ruíz

Moscoso

et al. 2015

Environ Microbiol Rep

View full text Add to dashboard Cite

Extracellular deoxyribonucleic acid (eDNA) is an essential component of bacterial biofilm matrices, and is required in their formation and maintenance. Extracellular DNA binds to exopolysaccharides or extracellular proteins, affording biofilms greater structural integrity. Recently, we reported evidence of intercellular eDNA-LytC complexes in pneumococcal biofilms. The LytC lysozyme is a member of the choline-binding family of proteins (CBPs) located on the pneumococcal surface. The present work shows that other CBPs, i.e. LytA, LytB, Pce, PspC and CbpF, which have a pI between 5 and 6, can bind DNA in vitro. This process requires the presence of divalent cations other than Mg(2+). This DNA binding capacity of CBPs appears to be independent of their enzymatic activity and, at least in the case of LytA, does not require the choline-binding domain characteristic of CBPs. Positively charged, surface-exposed, 25 amino acid-long peptides derived from the catalytic domain of LytB, were also found capable of DNA binding through electrostatic interactions. Confocal laser scanning microcopy revealed the existence of cell-associated LytB-eDNA complexes in Streptococcus pneumoniae biofilms. These and other findings suggest that these surface-located proteins of S. pneumoniae could play roles of varying importance in the colonization and/or invasion of human host where different environmental conditions exist.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Optimal Conditions For Cbp-dna Complex Formation In Vitromentioning

confidence: 99%

In vitro biofilm development of Streptococcus pneumoniae and formation of choline‐binding protein–DNA complexes

Domenech

Ruíz

Moscoso

et al. 2015

Environ Microbiol Rep

View full text Add to dashboard Cite

show abstract

“…AcpCD has a deep substrate‐binding groove constructed by three subdomains, the central subdomain, a relatively large arm subdomain, and an additional subdomain, giving a unique structure to AcpCD among GH73 family enzymes (Fig. S3) . Although the zymography analysis demonstrated that AcpCD does not exhibit species specificity, this structural feature of AcpCD may be favorable to hydrolyze the peptidoglycan of C. perfringens .…”

Section: Discussionmentioning

confidence: 99%

Structural and biochemical characterization of the Clostridium perfringens autolysin catalytic domain

et al. 2016

View full text Add to dashboard Cite

Bacterial autolysins can partially hydrolyze cell wall peptidoglycans into small sections to regulate cell separation/division and the growth phase. Clostridium perfringens autolysin (Acp) has an N-terminal cell wall-binding domain and a C-terminal catalytic domain with glucosaminidase activity that belongs to the glycoside hydrolase 73 family. Here, we determined the X-ray structure of the Acp catalytic domain (AcpCD) at 1.76 A resolution. AcpCD has a unique crescent-shaped structure, forming a deep groove for substratebinding at the center of the protein. The modeling study of the enzyme/substrate complex demonstrated that the length of the substrate-binding groove is closely related to the glucosaminidase activity. Mutagenesis analysis showed that AcpCD likely adopts a neighboring-group mechanism for the catalytic reaction.

show abstract

“…All share an ␣/␤-hydrolase-fold with a deep cleft that accommodates their glycan substrates and a conserved active site. With each, the identities of the catalytic acid/base residues is clear and they (21,49,50), together with the homolog of Staphylococcus warneri Atl (51), have been proven experimentally. These findings were confirmed in the current study with the significant decrease in catalytic activity found with S. typhimurium (Glu 184 3 Gln)FlgJ C .…”

Section: Discussionmentioning

confidence: 99%

The Essential Protein for Bacterial Flagella Formation FlgJ Functions as a β-N-Acetylglucosaminidase

Herlihey

Moynihan

Clarke

2014

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: FlgJ is required for flagella formation in Salmonella enterica. Results: The lytic activity of FlgJ was determined to be that of a ␤-N-acetylglucosaminidase using a novel assay. Conclusion: FlgJ is a hydrolase and not a lytic transglycosylase. Significance: This information is essential for the search and rational design of inhibitors that may serve as leads to a new class of antibiotics.

show abstract

Structure of Pneumococcal Peptidoglycan Hydrolase LytB Reveals Insights into the Bacterial Cell Wall Remodeling and Pathogenesis

Cited by 51 publications

References 62 publications

In vitro biofilm development of Streptococcus pneumoniae and formation of choline‐binding protein–DNA complexes

In vitro biofilm development of Streptococcus pneumoniae and formation of choline‐binding protein–DNA complexes

Structural and biochemical characterization of the Clostridium perfringens autolysin catalytic domain

The Essential Protein for Bacterial Flagella Formation FlgJ Functions as a β-N-Acetylglucosaminidase

Contact Info

Product

Resources

About