Modular design of the<i>Enterococcus hirae</i>muramidase-2 and<i>Streptococcus faecalis</i>autolysin

Joris, Bernard; Englebert, S.; Chu, Chien-Peng; Kariyama, Reiko; Daneo-Moore, L; Shockman, Gérald D.; Ghuysen, Jean‐Marie

doi:10.1111/j.1574-6968.1992.tb05218.x

Cited by 122 publications

(27 citation statements)

References 20 publications

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“…Other cell wall-associated bacterial proteins also carry repeated motifs at the C-terminal region to form ligand-binding domains (25,27,28). By analogy, it is likely that the N-terminal part of the AM domain of the staphylococcal autolysin, which is highly homologous to EJL AM and CWLA (see Fig.…”

Section: Discussionmentioning

confidence: 99%

A Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L-alanine amidase domain and an endo-beta-N-acetylglucosaminidase domain: cloning, sequence analysis, and characterization.

Oshida

Sugai

Komatsuzawa

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

275

296

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The Tn551 insertion site of the autolysisdeficient Staphylococcus aureus mutant RUSAL2 was cloned and used to identify the autolysis gene ati in the parent strain,RN450. The open reading frame for atl was 3768 bp in length, encoding a deduced protein of 1256 amino acids and molecular size of 137,381 Da. The atl gene product is a bifunctional protein that has an amidase domain and an endo-13-Nacetylglucosaminidase domain which must undergo proteolytic processing to generate the two extraceliular lytic enzymes found in the culture broth of S. aureus.

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Section: Discussionmentioning

confidence: 99%

A Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L-alanine amidase domain and an endo-beta-N-acetylglucosaminidase domain: cloning, sequence analysis, and characterization.

Oshida

Sugai

Komatsuzawa

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

275

296

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“…A 50-residue LysM domain occurs at the C terminus. The LysM domain is widespread in prokaryotes and is proposed to bind to peptidoglycan (42). It is found mainly in cell wall-degrading enzymes and is presumed to anchor catalytic domains to their substrates.…”

Section: Resultsmentioning

confidence: 99%

The Elastin-binding Protein of Staphylococcus aureus(EbpS) Is Expressed at the Cell Surface as an Integral Membrane Protein and Not as a Cell Wall-associated Protein

Downer¹,

Roche²,

Park³

et al. 2002

Journal of Biological Chemistry

133

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The elastin-binding proteins EbpS of Staphylococcus aureus strains Cowan and 8325-4 were predicted from sequence analysis to comprise 486 residues. Specific antibodies were raised against an N-terminal domain (residues 1-267) and a C-terminal domain (residues 343-486) expressed as recombinant proteins in Escherichia coli. Western blotting of lysates of wild-type 8325-4 and Newman and the corresponding ebpS mutants showed that EbpS migrated with an apparent molecular mass of 83 kDa. The protein was found exclusively in cytoplasmic membrane fractions purified from protoplasts or lysed cells, in contrast to the clumping factor ClfA, which was cell-wall-associated. EbpS was predicted to have three hydrophobic domains H1-(205-224), H2-(265-280), and H3-(315-342). A series of hybrid proteins was formed between EbpS at the N terminus and either alkaline phosphatase or ␤-galactosidase at the C terminus (EbpSPhoA, EbpS-LacZ). PhoA and LacZ were fused to EbpS between hydrophobic domains H1-H2 and H2-H3, and distal to H3. Expression of enzymatic activity in E. coli showed that EbpS is an integral membrane protein with two membrane-spanning domains H1 and H3. N-terminal residues 1-205 and C-terminal residues 343-486 were predicted to be exposed on the outer face of the cytoplasmic membrane. The ligand-binding domain of EbpS is known from previous studies to be present in the N terminus between residues 14 -34 and probing whole cells with anti-EbpS1-267 antibodies indicated that this region is exposed on the surface of intact cells. This was also confirmed by the observation that wildtype S. aureus Newman cells bound labeled tropoelastin whereas the ebpS mutant bound 72% less. In contrast, the C terminus, which carries a putative LysM peptidoglycan-binding domain, is not exposed on the surface of intact cells and presumably remains buried within the peptidoglycan. Finally, expression of EbpS was correlated with the ability of cells to grow to a higher density in liquid culture, suggesting that EbpS may have a role in regulating cell growth.

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“…The LysM motif is a common module found in many cell-wall degrading enzymes and proteins involved in bacterial pathogenesis and is often present in multiple repeats [9][10][11]. It has been proposed that the LysM-type cell-wall binding domain binds non-covalently to peptidoglycan of various gram-positive bacteria [12].…”

Section: The Protein Anchormentioning

confidence: 99%

Mucosal vaccine delivery of antigens tightly bound to an adjuvant particle made from food-grade bacteria

Roosmalen¹,

Kanninga²,

Khattabi³

et al. 2006

Methods

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102

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Modular design of theEnterococcus hiraemuramidase-2 andStreptococcus faecalisautolysin

Cited by 122 publications

References 20 publications

A Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L-alanine amidase domain and an endo-beta-N-acetylglucosaminidase domain: cloning, sequence analysis, and characterization.

A Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L-alanine amidase domain and an endo-beta-N-acetylglucosaminidase domain: cloning, sequence analysis, and characterization.

The Elastin-binding Protein of Staphylococcus aureus(EbpS) Is Expressed at the Cell Surface as an Integral Membrane Protein and Not as a Cell Wall-associated Protein

Mucosal vaccine delivery of antigens tightly bound to an adjuvant particle made from food-grade bacteria

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