Functional Inferences of Environmental Coccolithovirus Biodiversity
Functional Inferences of Environmental Coccolithovirus Biodiversity作者机构:Plymouth Marine LaboratoryProspect Place University of NottinghamSchool of BiosciencesSutton Bonington Campus Department of Biological ChemistryRothamsted Research School of Marine Science & EngineeringPlymouth University
出 版 物:《Virologica Sinica》 (中国病毒学(英文版))
年 卷 期:2013年第28卷第5期
页 面:291-302页
核心收录:
学科分类:07[理学] 09[农学] 0903[农学-农业资源与环境] 0713[理学-生态学]
基 金:funded by the NERC Oceans 2025 program Plymouth Marine Laboratory's Research Program the annual AMT program co-organised by the Plymouth Marine Laboratory the National Oceanographic Centre in Southampton
主 题:Coccolithovirus Major capsid protein Serine palmitoyltransferase Functional biodiversity
摘 要:The cosmopolitan calcifying alga Emiliania huxleyi is one of the most abundant bloom forming coccolithophore species in the oceans and plays an important role in global biogeochemical cycling. Coccolithoviruses are a major cause of coccolithophore bloom termination and have been studied in laboratory, mesocosm and open ocean studies. However, little is known about the dynamic interactions between the host and its viruses, and less is known about the natural diversity and role of functionally important genes within natural coccolithovirus communities. Here, we investigate the temporal and spatial distribution of coccolithoviruses by the use of molecular fingerprinting techniques PCR, DGGE and genomie sequencing. The natural biodiversity of the virus genes encoding the major capsid protein (MCP) and serine palmitoyltransferase (SPT) were analysed in samples obtained from the Atlantic Meridional Transect (AMT), the North Sea and the L4 site in the Westem Channel Observatory. We discovered nine new coccolithovirus genotypes across the AMT and L4 site, with the majority of MCP sequences observed at the deep chlorophyll maximum layer of the sampled sites on the transect. We also found four new SPT gene variations in the North Sea and at L4. Their translated fragments and the full protein sequence of SPT from laboratory strains EhV-86 and EhV-99B 1 were modelled and revealed that the theoretical fold differs among strains. Variation identified in the structural distance between the two domains of the SPT protein may have an impact on the catalytic capabilities of its active site. In summary, the combined use of 'standard' markers (i.e. MCP), in combination with metabolically relevant markers (i.e. SPT) are useful in the study of the phylogeny and functional biodiversity of coccolithoviruses, and can provide an interesting intracellular insight into the evolution of these viruses and their ability to infect and replicate within their algal hosts.