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Production of monoclonal antibodies against the major capsid protein of the Lactococcus bacteriophage ul36 and development of an enzyme-linked immunosorbent assay for direct phage detection in whey and milk

Article Abstract:

Monoclonal antibodies (MAbs) were raised against the major capsid protein of Lactococcus bacteriophage ul36, a member of the P335 species. The MAbs were used to develop an enzyme-linked immunosorbent assay which could be used for direct detection of phages in whey and milk without prior purification or enrichment. When combined with partial denaturation of a food sample, this procedure will greatly increase the sensitivity of detection of bacteriophages in food.

Author: Klaenhammer, Todd R., Moineau, Sylvain, Pandian, Sithian, Bernier, Denis, Jobin, Marie, Hebert, Jacques
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1993
Usage, Monoclonal antibodies, Enzyme-linked immunosorbent assay, Medical testing products, Diagnostic reagents and test kits, Diagnostic reagents

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Effect of increasing the copy number of bacteriophage origins of replication, in trans, on incoming-phage proliferation

Article Abstract:

Bacteriophage resistance mechanisms derived from a bacteriophage genome called Per (phage-encoded resistance) is present in Lactococcus lactis NCK203. Per50, cloned from phage phi-50, interferes with phi-50 duplications. The Per50 fragment provides little safe-guard to NCK203. Phi-50 infection is present in a low-copy-number plasmid pTRK 325. Per31 cloned from phage phi 31 enables replication of Per31-containing plasmids, in NCK203 or phi-31 infection.

Author: Klaenhammer, Todd R., Hill, Colin, O'Sullivan, Daniel J.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1993
Analysis, Chromosome replication

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The cell lysis activity of the streptococcus agalactiae bacteriophage B30 endolysin relies on the cysteine, histidine-dependent amidohydrolase/peptidase domain

Article Abstract:

The Streptococcus agalactiae bacteriophage B30 endolysin contains cysteine, histidine-dependent amidohydrolase/peptidase (CHAP), Acm glycosidase and the SH3b cell wall binding domain. Truncations and point mutations revealed that the Acm domain needs the SH3b domain for activity, whereas the CHAP domain is responsible for almost all cell lysis activity.

Author: Moineau, Sylvain, Donovan, David M., Dong, Shengli, Rousseau, Genevieve M., Pritchard, David G., Foster-Frey, Juli
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2006
United States, Science & research, Streptococcus agalactiae

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Subjects list: Research, Bacteriophages
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