Enzymatically active Peptostreptococcus magnus: association with site of infection

Infection of a prosthetic knee joint with Peptostreptococcus magnus.

Infection of a prosthetic knee joint with Peptostreptococcus magnus in an immunosuppressed patient with rheumatoid arthritis is described. The organism is a skin commensal, generally thought to be of low pathogenicity; the difficulty in making the diagnosis is emphasised.

Apparent culture-negative prosthetic valve endocarditis caused by Peptostreptococcus magnus.

In two patients with prosthetic valve endocarditis due to Peptostreptococcus magnus, blood cultures in the BacT/Alert and BACTEC 9240 systems were signal negative. The capability of the BacT/Alert system to detect various Peptostreptococcus species was assessed. P. magnus and P. anaerobius could not be detected, and subcultures remained negative. The growth in conventional media of these two sp...

Immunoglobulin-binding domains: Protein L from Peptostreptococcus magnus.

Protein L is a multidomain cell-wall protein isolated from Peptostreptococcus magnus. It belongs to a group of proteins that contain repeated domains that are able to bind to Igs without stimulating an immune response, the most characterized of this group being Protein A ( Staphylococcus aureus ) and Protein G ( Streptococcus ). Both of these proteins bind predominantly to the interface of C(H)...

Single-site mutations induce 3D domain swapping in the B1 domain of protein L from Peptostreptococcus magnus.

BACKGROUND Thermodynamic and kinetic studies of the Protein L B1 domain (Ppl) suggest a folding pathway in which, during the folding transition, the first beta hairpin is formed while the second beta hairpin and the alpha helix are largely unstructured. The same mutations in the two beta turns have opposite effects on the folding and unfolding rates. Three of the four residues composing the sec...

PROBING THE ACTIVE SITE OF RHODANESE WITH DISULFIDE REAGENTS