PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “Staphylococcus Phages”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 127 records · Page 7Linked to original sources
PubMed1994

Staphylococcus aureus phage typing, antimicrobial susceptibility patterns and patient data correlated using a personal computer: advantages for monitoring the epidemiology of MRSA.

Staphylococcus aureus, especially methicillin-resistant S. aureus (MRSA) is an important nosocomial pathogen. A problem encountered in the control of staphylococcal nosocomial infection is the difficulty correlating data available from antimicrobial susceptibility patterns (usually available locally) with phage typing patterns which are generally determined in a reference laboratory. Data problems are exaggerated because many patients have numerous samples taken over long periods of time. This paper describes the use of a database, 'DataEase', on a personal computer to correlate available data with patient demographics and to present the resulting information in whatever format is required. The information might be presented as the phage pattern of each isolate from patients in a particular unit per month or as a combination of the phage types and antimicrobial susceptibility patterns of isolates from a particular unit. The system can be used to generate a list of all isolates for phage typing in a format that allows the phage typing pattern to be recorded directly onto the list worksheet. In addition to providing clinically relevant reports, the system simplifies the collation of epidemiological information, data from which showed that since 1987 the incidence of MRSA has been rising in the group of hospitals served by this laboratory; MRSA of phage type 83A became a problem during 1990 and 1991; the incidence of gentamicin-sensitive phage type non-typable MRSA increased fourfold between 1988 and 1991; and the incidence of gentamicin-resistant MRSA rose sharply in 1992.

Bacteriophage Typing↗
PubMed1987

In vivo glycocalyx expression by Staphylococcus aureus phage type 52/52A/80 in S. aureus osteomyelitis.

Osteomyelitic rat tibiae were examined by scanning electron microscopy for the extracellular glycocalyx of Staphylococcus aureus. S. aureus and fractured tibiae from normal rats were incubated together in vitro and examined similarly. Low magnification of endosteal Haversian portals from tibiae studied in vivo and in vitro disclosed adherent S. aureus exuding glycocalyx that buried the organism in dense, coccoid-studded biofilms. The biofilm became progressively more dense over time in vitro and was exuberant at day 70 in vivo. S. aureus incubated in vitro without tibiae disclosed no glycocalyx. Bone chips studied in vitro disclosed staphylococci more commonly near the endosteal Haversian portals than on the intervening endosteal surfaces (mean +/- SE, 280 +/- 75 vs. 12 +/- 3 per 2,500-micron 2 field; P less than .002 by Student's t test). Organisms within ostia were not counted, although they occluded 10%-40% of the ostium. Staphylococci were adherent to exposed woven material, perhaps collagen.

Animals↗
PubMed1989

[The action of phage 52A on energy processes in Staphylococcus aureus].

Phage infection leads to the dissipation of the transmembrane difference of electric potentials, measured by the adsorption of lipophilic permeant ions of tetraphenyl phosphonium, in staphylococci. Besides, the reversible stimulation of cell respiration processes is observed. The duration of these effects is comparable with the period of the injection of phage DNA, equal to 2-3 minutes.

Adsorption↗
PubMed1999

Comparative sequence analysis of the DNA packaging, head, and tail morphogenesis modules in the temperate cos-site Streptococcus thermophilus bacteriophage Sfi21.

The temperate Streptococcus thermophilus bacteriophage Sfi21 possesses 15-nucleotide-long cohesive ends with a 3' overhang that reconstitutes a cos-site with twofold hyphenated rotational symmetry. Over the DNA packaging, head and tail morphogenesis modules, the Sfi21 sequence predicts a gene map that is strikingly similar to that of lambdoid coliphages in the absence of any sequence similarity. A nearly one to one gene correlation was found with the phage lambda genes Nu1 to H, except for gene B-to-E complex, where the Sfi21 map resembled that of coliphage HK97. The similarity between Sfi21 and HK97 was striking: both major head proteins showed an N-terminal coiled-coil structure, the mature major head proteins started at amino acid positions 105 and 104, respectively, and both major head genes were preceded by genes encoding a possible protease and portal protein. The purported Sfi21 protease is the first viral member of the ClpP protease family. The prediction of Sfi21 gene functions by reference to the gene map of intensively investigated coliphages was experimentally confirmed for the major head and tail gene. Phage Sfi21 shows nucleotide sequence similarity with Lactococcus phage BK5-T and a lactococcal prophage and amino acid sequence similarity with the Lactobacillus phage A2 and the Staphylococcus phage PVL. PVL is a missing link that connects the portal proteins from Sfi21 and HK97 with respect to sequence similarity. These observations and database searches, which demonstrate sequence similarity between proteins of phage from gram-positive bacteria, proteobacteria, and Archaea, constrain models of phage evolution.

Amino Acid Sequence↗
PubMed1999

Evidence for a holin-like protein gene fully embedded out of frame in the endolysin gene of Staphylococcus aureus bacteriophage 187.

We have cloned, sequenced, and characterized the genes encoding the lytic system of the unique Staphylococcus aureus phage 187. The endolysin gene ply187 encodes a large cell wall-lytic enzyme (71.6 kDa). The catalytic site, responsible for the hydrolysis of staphylococcal peptidoglycan, was mapped to the N-terminal domain of the protein by the expression of defined ply187 domains. This enzymatically active N terminus showed convincing amino acid sequence homology to an N-acetylmuramoyl-L-alanine amidase, whereas the C-terminal part, whose function is unknown, revealed striking relatedness to major staphylococcal autolysins. An additional reading frame was identified entirely embedded out of frame (+1) within the 5' region of ply187 and was shown to encode a small, hydrophobic protein of holin-like function. The hol187 gene features a dual-start motif, possibly enabling the synthesis of two products of different lengths (57 and 55 amino acids, respectively). Overproduction of Hol187 in Escherichia coli resulted in growth retardation, leakiness of the cytoplasmic membrane, and loss of de novo ATP synthesis. Compared to other holins identified to date, Hol187 completely lacks the highly charged C terminus. The secondary structure of the polypeptide is predicted to consist of two small, antiparallel, hydrophobic, transmembrane helices. These are supposed to be essential for integration into the membrane, since site-specific introduction of negatively charged amino acids into the first transmembrane domain (V7D G8D) completely abolished the function of the Hol187 polypeptide. With antibodies raised against a synthetic 18-mer peptide representing a central part of the protein, it was possible to detect Hol187 in the cytoplasmic membrane of phage-infected S. aureus cells. An important indication that the protein actually functions as a holin in vivo was that the gene (but not the V7D G8D mutation) was able to complement a phage lambda Sam mutation in a nonsuppressing E. coli HB101 background. Plaque formation by lambdagt11::hol187 indicated that both phage genes have analogous functions. The data presented here indicate that a putative holin is encoded on a different reading frame within the enzymatically active domain of ply187 and that the holin is synthesized during the late stage of phage infection and found in the cytoplasmic membrane, where it causes membrane lesions which are thought to enable access of Ply187 to the peptidoglycan of phage-infected Staphylococcus cells.

Amino Acid Sequence↗