title: Bacterial serine protease HtrA as a promising new target for antimicrobial therapy?
abstract: Recent studies have demonstrated that the bacterial chaperone and serine protease high temperature requirement A (HtrA) is closely associated with the establishment and progression of several infectious diseases. HtrA activity enhances bacterial survival under stress conditions, but also has direct effects on functions of the cell adhesion protein E-cadherin and extracellular matrix proteins, including fibronectin and proteoglycans. Although HtrA cannot be considered as a pathogenic factor per se, it exhibits favorable characteristics making HtrA a potentially attractive drug target to combat various bacterial infections.
authors.affiliation: Department of Molecular Biology, Division of Microbiology, Paris-Lodron University of Salzburg, Billroth Str. 11, A-5020, Salzburg, Austria. silja.wessler@sbg.ac.at.
authors.forename: Silja
authors.identifier: http://orcid.org/0000-0001-7011-6162
authors.initials: S
authors.lastname: Wessler
authors.affiliation: Department of Chemistry and Applied Biosciences, Swiss Federal Institute of Technology (ETH), Vladimir-Prelog-Weg 4, CH-8093, Zürich, Switzerland.
authors.forename: Gisbert
authors.initials: G
authors.lastname: Schneider
authors.affiliation: Division of Microbiology, University of Erlangen-Nuremberg, Staudtstr. 5, D-91058, Erlangen, Germany.
authors.forename: Steffen
authors.initials: S
authors.lastname: Backert
mesh_terms: D000890:Anti-Infective Agents / Q000494:pharmacology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D000072417:Protein Domains; D057057:Serine Proteases / Q000737:chemistry / Q000378:metabolism*
chemical_list: D000890:Anti-Infective Agents; D001426:Bacterial Proteins; D057057:Serine Proteases