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Biomedical subjects

Laura Selan

Publications and source records attributed to Laura Selan.

3 recordsLinked to original sources

A microbiological and confocal microscopy study documenting a slime-producing Staphylococcus epidermidis isolated from a nylon corneal suture of a patient with antibiotic-resistant endophthalmitis.

BACKGROUND: We describe a case of posttraumatic endophthalmitis unresponsive to systemic (amoxicillin+clavulanic acid and piperacillin/tazobactam), intra-ocular (vancomycin) and topical (ofloxacin, tetracycline and sulfametoxazole) antibiotic therapy. Microbiological and confocal microscopy studies of a nylon corneal suture revealed the presence of a slime-producing strain of Staphylococcus epidermidis. METHODS: We describe the history and clinical presentation of a 77-year-old man in whom a high-grade posttraumatic endophthalmitis resolved only after the removal of a single nylon corneal suture. Microbiological investigations of the aqueous, vitreous and suture were performed, and the propensity of the suture-associated isolate to form biofilm was assessed using confocal microscopy. RESULTS: A single stain of S. epidermidis was isolated from both aqueous and vitreous specimens and from the suture. The planktonic form of the isolate was susceptible in vitro to the antibiotics administered to the patient, but the strain was capable of forming biofilms and this phenotype showed resistance to high concentrations of the same antibiotics. CONCLUSIONS: The presence of a slime-producing strain of S. epidermidis should be considered in endophthalmitis that is unresponsive to specific antibiotic therapy, especially in cases in which an intra-ocular foreign body (e.g., a suture) is present.

Aged↗

Diagnosis of vascular graft infections with antibodies against staphylococcal slime antigens.

Late-onset infections of synthetic vascular grafts (LO-SVGIs) are generally caused by staphylococci that produce a slime polysaccharide and grow as a biofilm on the graft surface. We developed an ELISA to detect serum antibodies against staphylococcal slime polysaccharide antigens (SSPA). Patients with an ongoing staphylococcal LO-SVGI had greater titres of IgM antibodies against SSPA than did patients in other groups. Antibody titres of 0.40 ELISA units (EU) or more, or 0.35 EU or more detected 97% and 100% of staphylococcal LO-SVGIs, respectively, 0% and 2% titre/unit false-positive results. Our findings suggest that such an ELISA represents a sensitive, specific, and non-invasive diagnostic test for staphylococcal LO-SVGIs.

Antibodies, Bacterial↗

The Chryseobacterium meningosepticum PafA enzyme: prototype of a new enzyme family of prokaryotic phosphate-irrepressible alkaline phosphatases?

Chryseobacterium meningosepticum is an aerobic Gram-negative rod widely distributed in natural environments. Unlike many bacteria, it produces a phosphate-irrepressible periplasmic alkaline phosphatase (AP). This work describes cloning of the gene encoding that enzyme from C. meningosepticum CCUG 4310 (NCTC 10585), and preliminary characterization of its product. The gene, named pafA, encodes a protein (PafA) of 546 amino acids with a calculated molecular mass of the mature peptide of 58682 Da. PafA exhibits high sequence identity with the PhoV AP of Synechococcus PCC 7942 (49.9% identity) and with the Cda Ca(2+)-dependent ATPase of Myroides odoratus (51.9% identity), while being more distantly related to the PhoD AP of Zymomonas mobilis (22.1% identity) and to the PhoA AP of Escherichia coli (14.0% identity). PafA was partially purified; it exhibits optimal activity at pH 8.5 and is active towards a broad spectrum of substrates including both phosphomonoesters and ATP, with preferential activity for the latter compound. The present findings allow definition of a new family of APs including 60 kDa, periplasmic enzymes whose expression is not influenced by freely available P(i) in the medium. Moreover, PafA can be considered an evolutionary intermediate between Ca(2+)-ATPase of M. odoratus and the APs PhoV of Synechococcus PCC 7942 and PhoD of Z. mobilis.

Alkaline Phosphatase↗