Extracellular Protein A from a Methicillin‐Resistant Strain of <i>Staphylococcus aureus</i>

Lindmark, Roger; Movitz, Jan; Sjöquist, John

doi:10.1111/j.1432-1033.1977.tb11431.x

Cited by 67 publications

(17 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This means that S. aureus has at least two proteins recognizing vWf, one cell-surface-attached and one secreted as reported in this paper. To further complicate the picture, it has been reported that protein A in some strains exists in a soluble form, not bound to the surface of S. aureus (Lindmark et al, 1977). The function and importance of vWpb during S. aureus infections is not yet known.…”

Section: Possible Consequences Of the Interaction Between S Aureus Amentioning

confidence: 99%

A novel von Willebrand factor binding protein expressed by Staphylococcus aureus a aThe GenBank accession number for the sequence reported in this paper is AY032850.

et al. 2002

View full text Add to dashboard Cite

When a shotgun phage-display library of Staphylococcus aureus Newman was affinity selected (panned) against recombinant von Willebrand factor (vWf), a novel von Willebrand factor binding protein (vWbp) was found. Experimental data indicate that the interaction between vWbp and vWf is very specific and mediated by a region of 26 aa residues in the C-terminal part of vWbp. vWbp has an N-terminal secretory signal sequence but no cell wall anchoring motif, suggesting a soluble extracellular location. Mature vWbp could be purified from the culture supernatant and the identity of the protein was confirmed by N-terminal sequencing. vWbp migrates with an apparent molecular mass of 66 kDa and the deduced protein consists of 482 aa. The gene encoding vWbp, named vwb, was present in all S. aureus strains investigated.

show abstract

Section: Possible Consequences Of the Interaction Between S Aureus Amentioning

confidence: 99%

A novel von Willebrand factor binding protein expressed by Staphylococcus aureus a aThe GenBank accession number for the sequence reported in this paper is AY032850.

et al. 2002

View full text Add to dashboard Cite

show abstract

“…However, a small portion of SPA can be released into the extracellular environment during exponential growth in vitro (45)(46)(47). Some strains of MRSA produce only extracellular protein A (48). The release mechanism is unknown and the significance has not been previously evaluated in vivo.…”

Section: Chemokinementioning

confidence: 99%

Host Chemokines Bind to Staphylococcus aureus and Stimulate Protein A Release

Yung

Parenti

Murphy

2011

Journal of Biological Chemistry

View full text Add to dashboard Cite

There are few examples of host signals that are beneficial to bacteria during infection. Here we found that 31 out of 42 host immunoregulatory chemokines were able to induce release of the virulence factor protein A (SPA) from a strain of community-associated methicillin-resistant Staphylococcus aureus (CA-MRSA). Detailed study of chemokine CXCL9 revealed that SPA release occurred through a post-translational mechanism and was inversely proportional to bacterial density. CXCL9 bound specifically to the cell membrane of CA-MRSA, and the related SPA-releasing chemokine CXCL10 bound to both cell wall and cell membrane. Clinical samples from patients infected with S. aureus and samples from a mouse model of CA-MRSA skin abscess all contained extracellular SPA. Further, SPA-releasing chemokines were present in mouse skin lesions infected with CA-MRSA. Our data identify a potential new mode of immune evasion, in which the pathogen exploits a host defense factor to release a virulence factor; moreover, chemokine binding may serve a scavenging function in immune evasion by S. aureus.

show abstract

“…This should be reflected by the presence of a C-terminal structure in region C not homologous to corresponding subregions in regions D, A, and B, which, however is not the case. The problem may be solved by sequence analysis of proteinA from bacterial mutants which do not exhibit blocked N-termini [29,30].…”

Section: The Proposed Primary Structure Of the Total Fc-binding Portimentioning

confidence: 99%

Structural Studies on the Four Repetitive Fc-Binding Regions in Protein A from Staphylococcus aureus

Sjödahl¹

1977

Eur J Biochem

121

View full text Add to dashboard Cite

The covalent structures of the four highly homologous Fc-binding regions in protein A, regions D, A, B, and C, have been studied by enzymic fragmentations of previously isolated fragments originating from these regions and subsequent isolation of the generated peptides by ion-exchange chromatography, molecular-sieve chromatography, high-voltage paper electrophoresis and paper chromatography. The complete sequence of region B was elucidated by combining the results of Edman degradations on isolated fragment B peptides with the previously reported N-terminal sequence of the same fragment. Furthermore, Edman degradations of fragment D, A and C peptides differing from the region B sequence provided the structures of subregions not identical to corresponding subregions within region B. Thus, it is possible to propose a highly probable covalent structure for the N-terminal 27 000-molecular-weight portion of protein A responsible for the IgG-Fc-binding activities. However, it was not possible to assign the activities to specific structures within the regions.The sequence data indicate that not only mutual homology between the four regions exists, but also internal homologies within the regions. Furthermore, the data strongly supports the hypothesis of a stepwise gene fusion procedure being involved in the evolution of the protein.

show abstract

Extracellular Protein A from a Methicillin‐Resistant Strain of Staphylococcus aureus

Cited by 67 publications

References 31 publications

A novel von Willebrand factor binding protein expressed by Staphylococcus aureus a aThe GenBank accession number for the sequence reported in this paper is AY032850.

A novel von Willebrand factor binding protein expressed by Staphylococcus aureus a aThe GenBank accession number for the sequence reported in this paper is AY032850.

Host Chemokines Bind to Staphylococcus aureus and Stimulate Protein A Release

Structural Studies on the Four Repetitive Fc-Binding Regions in Protein A from Staphylococcus aureus

Contact Info

Product

Resources

About