Systematic analysis of an amidase domain CHAP in 12 Staphylococcus aureus genomes and 44 staphylococcal phage genomes

Zou, Yanming; Hou, Chun

doi:10.1016/j.compbiolchem.2010.07.001

Cited by 27 publications

(25 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Residues 160 through 225 represented the bacterial Src homology 3 (SH3) domain (pfam08239; superfamily cl02551) that bind to target proteins through sequences containing proline and hydrophobic amino acids. The cell wall targeting-SH3 domains are associated with other hydrolases such as the phage associated cysteine, histidine-dependent amidohydrolase/peptidases (CHAPs), but does not contain the N-terminal ‘F-[IV]-R’ motif common to staphylococcal bacteriophage CHAPs [37], [38]. Interestingly, the C-terminal SH3 portion of the bacteriophage lysins aligned most closely with bacterial CHAP domains, specifically a glycosyl hydrolase, family 25-protein from C. perfringens [e.g., ZP_02642156 and seventeen other related sequences].…”

Section: Resultsmentioning

confidence: 99%

Molecular Characterization of Podoviral Bacteriophages Virulent for Clostridium perfringens and Their Comparison with Members of the Picovirinae

et al. 2012

View full text Add to dashboard Cite

Clostridium perfringens is a Gram-positive, spore-forming anaerobic bacterium responsible for human food-borne disease as well as non-food-borne human, animal and poultry diseases. Because bacteriophages or their gene products could be applied to control bacterial diseases in a species-specific manner, they are potential important alternatives to antibiotics. Consequently, poultry intestinal material, soil, sewage and poultry processing drainage water were screened for virulent bacteriophages that lysed C. perfringens. Two bacteriophages, designated ΦCPV4 and ΦZP2, were isolated in the Moscow Region of the Russian Federation while another closely related virus, named ΦCP7R, was isolated in the southeastern USA. The viruses were identified as members of the order Caudovirales in the family Podoviridae with short, non-contractile tails of the C1 morphotype. The genomes of the three bacteriophages were 17.972, 18.078 and 18.397 kbp respectively; encoding twenty-six to twenty-eight ORF's with inverted terminal repeats and an average GC content of 34.6%. Structural proteins identified by mass spectrometry in the purified ΦCP7R virion included a pre-neck/appendage with putative lyase activity, major head, tail, connector/upper collar, lower collar and a structural protein with putative lysozyme-peptidase activity. All three podoviral bacteriophage genomes encoded a predicted N-acetylmuramoyl-L-alanine amidase and a putative stage V sporulation protein. Each putative amidase contained a predicted bacterial SH3 domain at the C-terminal end of the protein, presumably involved with binding the C. perfringens cell wall. The predicted DNA polymerase type B protein sequences were closely related to other members of the Podoviridae including Bacillus phage Φ29. Whole-genome comparisons supported this relationship, but also indicated that the Russian and USA viruses may be unique members of the sub-family Picovirinae.

show abstract

Section: Resultsmentioning

confidence: 99%

Molecular Characterization of Podoviral Bacteriophages Virulent for Clostridium perfringens and Their Comparison with Members of the Picovirinae

et al. 2012

View full text Add to dashboard Cite

show abstract

“…SsaA has been linked to the hypersensitivity to macrolide-lincosamide-streptogramin B antibiotics of a thermosensitive walRK mutant in S. aureus , though the underlying molecular mechanism is unknown [45]. CHAP domains are conserved in a subset of peptidoglycan hydrolases [23], [24], [34], [35] and we have identified 14 genes encoding CHAP-domain proteins in the S. aureus NCTC 8325 genome [5], and shown that six of these are regulated by the WalKR system [14] and (A. Delaune et al ., in preparation). Of these, only ssaA is able to compensate for the absence of WalKR when it is overexpressed (Fig.…”

Section: Discussionmentioning

confidence: 99%

Peptidoglycan Crosslinking Relaxation Plays an Important Role in Staphylococcus aureus WalKR-Dependent Cell Viability

et al. 2011

View full text Add to dashboard Cite

The WalKR two-component system is essential for viability of Staphylococcus aureus, a major pathogen. We have shown that WalKR acts as the master controller of peptidoglycan metabolism, yet none of the identified regulon genes explain its requirement for cell viability. Transmission electron micrographs revealed cell wall thickening and aberrant division septa in the absence of WalKR, suggesting its requirement may be linked to its role in coordinating cell wall metabolism and cell division. We therefore tested whether uncoupling autolysin gene expression from WalKR-dependent regulation could compensate for its essential nature. Uncoupled expression of genes encoding lytic transglycosylases or amidases did not restore growth to a WalKR-depleted strain. We identified only two WalKR-regulon genes whose expression restored cell viability in the absence of WalKR: lytM and ssaA. Neither of these two genes are essential under our conditions and a ΔlytM ΔssaA mutant does not present any growth defect. LytM is a glycyl–glycyl endopeptidase, hydrolyzing the pentaglycine interpeptide crossbridge, and SsaA belongs to the CHAP amidase family, members of which such as LysK and LytA have been shown to have D-alanyl-glycyl endopeptidase activity, cleaving between the crossbridge and the stem peptide. Taken together, our results strongly suggest that peptidoglycan crosslinking relaxation through crossbridge hydrolysis plays a crucial role in the essential requirement of the WalKR system for cell viability.

show abstract

“…More recently, computer-based analysis of VAPGHs amino acids sequences from different phages infecting S. aureus revealed a high similarity between these proteins (Rodríguez et al, 2011). Moreover, endolysins encoded by staphylococcal phages, and particularly the CHAP domain, presented a conserved sequence also found in bacterial PG hydrolytic proteins (Zou and Hou, 2010). This would not be surprising because they all share the same PG substrate.…”

Section: Evolutionary Insightsmentioning

confidence: 94%

Bacteriophage virion-associated peptidoglycan hydrolases: potential new enzybiotics

Rodríguez-Rubio

Martínez

Donovan³

et al. 2012

Critical Reviews in Microbiology

135

110

View full text Add to dashboard Cite

Virion-associated peptidoglycan hydrolases (VAPGH) are phage-encoded lytic enzymes that locally degrade the peptidoglycan (PG) of the bacterial cell wall during infection. In contrast to endolysins, PGHs that mediate lysis of the host bacteria at the end of the lytic cycle to release of phage progeny, the action of VAPGHs generates a small hole through which the phage tail tube crosses the cell envelope to eject the phage genetic material at the beginning to the infection cycle. The antimicrobial activity of VAPGHs was first discovered through the observation of the phenomenon of 'lysis from without', in which the disruption of the bacterial cell wall occurs prior to phage production and is caused by a high number of phages adsorbed onto the cell surface. Based on a unique combination of properties of VAPGHs such as high specificity, remarkable thermostability, and a modular organization, these proteins are potential candidates as new antibacterial agents, e.g. against antibiotic-resistant bacteria in human therapy and veterinary as well as biopreservatives in food safety, and as biocontrol agents of harmful bacteria in agriculture. This review provides an overview of the different VAPGHs discovered to date and their potential as novel antimicrobials.

show abstract

Systematic analysis of an amidase domain CHAP in 12 Staphylococcus aureus genomes and 44 staphylococcal phage genomes

Cited by 27 publications

References 35 publications

Molecular Characterization of Podoviral Bacteriophages Virulent for Clostridium perfringens and Their Comparison with Members of the Picovirinae

Molecular Characterization of Podoviral Bacteriophages Virulent for Clostridium perfringens and Their Comparison with Members of the Picovirinae

Peptidoglycan Crosslinking Relaxation Plays an Important Role in Staphylococcus aureus WalKR-Dependent Cell Viability

Bacteriophage virion-associated peptidoglycan hydrolases: potential new enzybiotics

Contact Info

Product

Resources

About