Draft Genome Sequence of Lactococcus lactis Strain PrHT3, Isolated from Organic Basil.

Here, we report the draft genome sequence of Lactococcus lactis strain PrHT3, which was isolated from organic basil. This strain possesses one chromosome and two plasmids. This strain possesses potential probiotic characteristics.

Draft Genome Sequences of the Vibrio parahaemolyticus Strains VHT1 and VHT2, Pasteurization-Resistant Isolates from Environmental Seafood.

Two pasteurization-resistant strains, VHT1 and VHT2, of environmental, viable but nonculturable, pathogenic Vibrio parahaemolyticus were isolated from environmental oysters. Their whole-genome sequences were constructed. The genome sizes for VHT1 and VHT2 are 5.

Recovery of Pasteurization-Resistant from Seafoods Using a Modified, Two-Step Enrichment.

Persistent Vibrio-parahaemolyticus-associated vibriosis cases, attributed, in part, to the inefficient techniques for detecting viable-but-non-culturable (VBNC) Vibrio pathogens and the ingestion of undercooked seafood, is the leading cause of bacterial seafood-borne outbreaks, hospitalizations, and deaths in the United States. The effect of extreme heat processing on Vibrio biology and its potential food safety implication has been underexplored. In the present work, environmental samples from the wet market, lagoon, and estuarine environments were analyzed for V.

RT-qPCR Analysis of 15 Genes Encoding Putative Surface Proteins Involved in Adherence of Listeria monocytogenes.

adherence to food-associated abiotic surfaces and the development of biofilms as one of the underlying reasons for the contamination of ready-to-eat products is well known. The over-expression of internalins that improves adherence has been noted in cells growing as attached cells or at elevated incubation temperatures. However, the role of other internalin-independent surface proteins as adhesins has been uncharacterized to date.

Comparison of Surface Proteomes of Adherence Variants of Listeria Monocytogenes Using LC-MS/MS for Identification of Potential Surface Adhesins.

The ability of Listeria monocytogenes to adhere and form biofilms leads to persistence in food processing plants and food-associated listeriosis. The role of specific surface proteins as adhesins to attach Listeria cells to various contact surfaces has not been well characterized to date. In prior research comparing different methods for surface protein extraction, the Ghost urea method revealed cleaner protein content as verified by the least cytoplasmic protein detected in surface extracts using LC-MS/MS.

Comparison of five methods for direct extraction of surface proteins from Listeria monocytogenes for proteomic analysis by orbitrap mass spectrometry.

Extracts of surface proteins, with minimal artifacts from contaminating cytosolic components, are highly desirable for investigating surface factors involved in the attachment and formation of biofilms by bacteria that are problematic in commercial food processing facilities. In this study, we compared the protein profiles of the food pathogen, Listeria monocytogenes, recovered after applying different surface protein extraction methods compiled from the literature: trypsin-enzymatic shaving with BICAM/sucrose or Tris/sucrose buffers (Tryp B+S, Tryp T+S), Tris-buffered urea (UB), lithium chloride (LiCl) and Tris-buffered urea applied with hypotonic-stressed cells (UB-Ghost), and subjected them to liquid chromatography tandem mass spectrometry and protein identification. The data indicate that the UB-Ghost extraction method provides a cleaner extract of surface proteins including the predicted (this study and the literature) or validated members (literature) from L.