Abstract:
BACKGROUND:The life cycle of a bacteriophage has tightly programmed steps to help virus infect its host through the interactions between the bacteriophage and its host proteins. However, bacteriophage-host protein interactions in high temperature environment remain poorly understood. To address this issue, the protein interaction between the thermophilic bacteriophage GVE2 and its host thermophilic Geobacillus sp. E263 from a deep-sea hydrothermal vent was characterized. RESULTS:This investigation showed that the host's aspartate aminotransferase (AST), chaperone GroEL, and viral capsid protein VP371 formed a linearly interacted complex. The results indicated that the VP371-GroEL-AST complex were up-regulated and co-localized in the GVE2 infection of Geobacillus sp. E263. CONCLUSIONS:As reported, the VP371 is a capsid protein of GVE2 and the host AST is essential for the GVE2 infection. Therefore, our study revealed that the phage could use the anti-stress system of its host to protect the virus reproduction in a high-temperature environment for the first time.
journal_name
BMC Microbioljournal_title
BMC microbiologyauthors
Chen Y,Wei D,Wang Y,Zhang Xdoi
10.1186/1471-2180-13-48subject
Has Abstractpub_date
2013-02-26 00:00:00pages
48issn
1471-2180pii
1471-2180-13-48journal_volume
13pub_type
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