A coagulase-negative and non-haemolytic strain of Staphylococcus aureus for investigating the roles of SrtA in a murine model of bloodstream infection.

Sortase A (SrtA) is a cysteine transpeptidase and virulence factor from Staphylococcus aureus (S. aureus) that catalyses the attachment and display of surface proteins on the cell wall, thereby mediating bacterial adhesion to host tissues, host-cell entry and evasion of the immune response. As a result, SrtA has become an important target in the development of therapies for S.

Quercitrin, an inhibitor of Sortase A, interferes with the adhesion of Staphylococcal aureus.

Sortase A (SrtA) is a cysteine transpeptidase of most Gram-positive bacteria that is responsible for the anchorage of many surface protein virulence factors to the cell wall layer. SrtA mutants are unable to display surface proteins and are defective in the establishment of infections without affecting microbial viability. In this study, we report that quercitrin (QEN), a natural compound that does not affect Staphylococcus aureus growth, can inhibit the catalytic activity of SrtA in fibrinogen (Fg) cell-clumping and immobilized fibronectin (Fn) adhesion assays.

Externally controlled triggered-release of drug from PLGA micro and nanoparticles.

Biofilm infections are extremely hard to eradicate and controlled, triggered and controlled drug release properties may prolong drug release time. In this study, the ability to externally control drug release from micro and nanoparticles was investigated. We prepared micro/nanoparticles containing ciprofloxacin (CIP) and magnetic nanoparticles encapsulated in poly (lactic-co-glycolic acid) PLGA.

Production and characterization of mouse monoclonal antibodies against lysis protein E of phiX174.

Bacterial ghosts offer a new avenue for the study of inactivated vaccines. However, for many years the mechanism of genetic inactivation was controversial. To obtain mouse monoclonal antibodies (mAbs) against protein E will allow the observation of its location and dynamic expression to expand understanding of the lysis mechanism.

Enhancement of bacteriolysis of shuffled phage PhiX174 gene E.

Bacterial ghosts that are generated using the regulated PhiX174 lysis gene E offer a new avenue for the study of inactivated vaccines. Here, we constructed a library of mutant gene E using a gene-shuffling technique. After screening and recombination with the prokaryotic non-fusion expression vector pBV220, two lysis plasmids were selected.

Salmonella enteritidis ghost vaccine induces effective protection against lethal challenge in specific-pathogen-free chicks.

Bacterial ghosts (BGs) are empty bacterial envelopes generated by expulsion of the bacterial genome and cytoplasmic contents from bacterial cells, and the process is mediated by lysis protein E encoded on bacteriophage PhiX174. BGs represent a new approach in vaccine development and have been applied to a variety of gram-negative bacterial vaccine candidates. In this study, a BG vaccine generated from Salmonella enteritidis (S.

[Expression, purification and antigen activity analysis of the N-terminal domain of lipoprotein LppQ of Mycoplasma mycoide subsp. mycoides SC].

The gene sequence coding the N-terminal domain of LppQ was amplified from Mycoplasma mycoides subsp. mycoides SC (MmmSC) HVRI X strain by PCR using special primers and was cloned into the EcoR I /Sal I sites of pET32a vector to construct the expression recombinant plasmids. The recombinant plasmids were indentified by restriction digestion, PCR and sequence analysis.