Draft Genome Sequence of a Methicillin-Resistant Sequence Type 39 Staphylococcal Isolate Obtained from Seafood.

The draft genome sequence of a methicillin-resistant (MRSA) sequence type 39 (ST 39) isolate obtained from the dried ribbonfish of Gujarat, India, is reported here. -specific genes were present in this MRSA isolate. The whole-genome sequence of this strain contains 2,693 protein-coding genes and 70 RNAs within the 2.

Draft Genome Sequence of a Methicillin-Resistant Isolate (Sequence Type 1) from Seafood.

The draft genome sequence of a methicillin-resistant (MRSA) isolate (sequence type 1 [ST 1]) from the salted dried ribbonfish from Gujarat, India, is reported here. genus-specific genes were present in this MRSA isolate. The whole-genome sequence of this strain contains 2,797 protein-coding genes and 80 RNAs within the 2.

Assessment of microbial quality of fish processing industrial effluent in bar-mouth at Bhidia landing site, Veraval, Gujarat, India.

The present study was carried out to assess the microbial quality of fish processing industries effluent at Bhidia bar-mouth, Veraval, Gujarat during April, 2012 to March 2013. The total viable bacterial count (TVBC), total Enterobacteriaceae count, E. coli count (EC), Staphylococcus aureus and Fecal Streptococcal count in effluent ranged from 3.

Polymorphism at residue 129 modulates the conformational conversion of the D178N variant of human prion protein 90-231.

One of the arguments in favor of the protein-only hypothesis of transmissible spongiform encephalopathies is the link between inherited prion diseases and specific mutations in the PRNP gene. One such mutation (Asp178 --> Asn) is associated with two distinct disorders: fatal familial insomnia or familial Creutzfeldt-Jakob disease, depending upon the presence of Met or Val at position 129, respectively. In this study, we have characterized the biophysical properties of recombinant human prion proteins (huPrP90-231) corresponding to the polymorphic variants D178N/M129 and D178N/V129.

Molecular basis of barriers for interspecies transmissibility of mammalian prions.

Spongiform encephalopathies are believed to be transmitted by a unique mechanism involving self-propagating conformational conversion of prion protein into a misfolded form. Here we demonstrate that fundamental aspects of mammalian prion propagation, including the species barrier and strain diversity, can be reproduced in vitro in a seeded fibrillization of the recombinant prion protein variant Y145Stop. Our data show that species-specific substitution of a single amino acid in a critical region completely changes the seeding specificity of prion protein fibrils.