Complete Genome Sequence of Virulence-Enhancing Siphophage VHS1 from Vibrio harveyi

Author:

Khemayan Krit12,Prachumwat Anuphap134,Sonthayanon Burachai14,Intaraprasong Aungkul125,Sriurairatana Siriporn1,Flegel Timothy W.124

Affiliation:

1. Centex Shrimp, Faculty of Science, Mahidol University, Bangkok, Thailand

2. Department of Biotechnology, Faculty of Science, Mahidol University, Bangkok, Thailand

3. Shrimp-Virus Interaction Laboratory, Agricultural Biotechnology Research Unit, National Center for Genetic Engineering and Biotechnology (BIOTEC), National Science and Technology Development Agency, Klong Luang, Pathumthani, Thailand

4. National Center for Genetic Engineering and Biotechnology (BIOTEC), National Science and Technology Development Agency, Klong Luang, Pathumthani, Thailand

5. Center of Excellence for Agricultural Biotechnology (AG-BIO/PERDO-CHE), Bangkok, Thailand

Abstract

ABSTRACT Vibrio harveyi siphophage 1 (VHS1) is a tailed phage with an icosahedral head of approximately 66 nm in diameter and an unornamented, flexible tail of approximately 153 nm in length. When Vibrio harveyi 1114GL is lysogenized with VHS1, its virulence for the black tiger shrimp ( Penaeus monodon ) increases by more than 100 times, and this coincides with production of a toxin(s) associated with shrimp hemocyte agglutination. Curiously, the lysogen does not show increased virulence for the whiteleg shrimp ( Penaeus [ Litopenaeus ] vannamei ). Here we present and annotate the complete, circular genome of VHS1 (81,509 kbp; GenBank accession number JF713456 ). By software analysis, the genome contains 125 putative open reading frames (ORFs), all of which appear to be located on the same DNA strand, similar to the case for many other bacteriophages. Most of the putative ORFs show no significant homology to known sequences in GenBank. Notable exceptions are ORFs for a putative DNA polymerase and putative phage structural proteins, including a portal protein, a phage tail tape measure protein, and a phage head protein. The last protein was identified as a component of the species-specific toxin mixture described above as being associated with agglutination of hemocytes from P. monodon .

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

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