Suitability of a recombinant Staphylococcus aureus enterotoxin C bovine variant for immunodiagnostics and therapeutic vaccine development.

Recombinant bovine variant of staphylococcal enterotoxin C (SECbovine), produced as a NH2-terminal histidine hexamer fusion protein (His6-tagged SECbovine), expressed at high levels (25%) in Escherichia coli and affinity purified to homogeneity (99.9%), was tested for its diagnostic and therapeutic potentials. His6-tagged SECbovine is antigenically authentic to native SECbovine across host species, as confirmed by antibody-based capture detection assays using human, mouse, rabbit and chicken hyperimmune sera.

Treatment efficacy of the lead RNAIII-inhibiting peptide YSPWTNF-NH2 in acquired Staphylococcus aureus sepsis: a histopathological assessment.

The quorum-sensing interfering RNAIII-inhibiting peptide (RIP) YSPXTNF and its synthetic analogues YSPWTNF and YSPITNF have been shown to prevent and suppress diseases caused by Staphylococcus aureus at different body sites in different animal models. This study was designed to investigate histopathologically the therapeutic efficacy of lead peptide RIP YSPWTNF-NH(2) in the subcutaneous air sac murine model of acquired S. aureus sepsis.

Prevention of lethal murine candidiasis using HP (2-20), an antimicrobial peptide derived from the N-terminus of Helicobacter pylori ribosomal protein L1.

Peptide HP (2-20), A(2)KKVFKRLEKLFSKIQNDK(20), is a cationic antimicrobial peptide derived from the N-terminus of Helicobacter pylori ribosomal protein 1, HpRpL1. Native peptide HP (2-20) and its synthetic derivatives have been shown in vitro to exhibit potent killing activity against Gram-positive, Gram-negative and yeast cells, thus, making them promising candidates for treatment of polymicrobial infections. However, the therapeutic potential of peptide HP (2-20) or its synthetic derivatives in any animal model of either bacterial or fungal diseases has not yet been investigated.