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United States Department of Agriculture

Agricultural Research Service

Research Project: Integrated Aquatic Animal Health Strategies

Location: Aquatic Animal Health Research

Title: Identification, phylogenetic relationships, characterization and gene expression patterns of six different annexins of channel catfish (Ictalurus punctatus Rafinesque, 1818)

Authors
item Yeh, Hung-Yueh
item Klesius, Phillip

Submitted to: Veterinary Immunology and Immunopathology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: March 2, 2010
Publication Date: June 4, 2010
Repository URL: http://handle.nal.usda.gov/10113/43327
Citation: Yeh, H., Klesius, P.H. 2010. Identification, phylogenetic relationships, characterization and gene expression patterns of six different annexins of channel catfish (Ictalurus punctatus Rafinesque, 1818). Veterinary Immunology and Immunopathology. 136: 176-183.

Interpretive Summary: Annexins are a group of proteins that are able to bind Ca++-dependent phospholipid-binding proteins. They are found in the living organisms except bacteria, and play many important roles in normal cellular processes. In our study of channel catfish infection with Edwardsiella ictaluri, we found six annexin genes (A1, A2, A4, A5, A6 and A11) were up-regulated at the early stage of infection. In this report, we sequenced and characterized these complimentary DNA (cDNA) transcripts. The full-length nucleic acid sequences of channel catfish annexins ranges from 1231 (annexin A1) to 2476 (annexin A6). Each cDNA transcript has one open reading, which appears to encode peptides ranges from 317 to 662 amino acid residues with the calculated molecular masses from 35.0 (annexin A5) to 74.5 kDa (annexin A6). Evolutionary and sequence analysis demonstrates that each channel catfish annexin had a diversified amino terminus, and had four structurally conserved 70-amino-acid repeats. In addition, several important features for annexin functions were conserved in channel catfish. For expression profile, channel catfish annexin A1, A4 and A6 transcripts were detected in spleen, anterior kidney, liver, intestine, skin and gill of fish examined. However, annexin A2, A5 and A11 cDNAs were variously detected in tissues of fish sampled. This result provides important information for further elucidating channel catfish annexin functions in vivo.

Technical Abstract: Annexins are Ca++-dependent phospholipid-binding proteins. They are ubiquitous in living organisms and are involved in many cellular processes. In the course of studying Edwardsiella ictaluri pathogenesis in channel catfish, we identified that six annexin expressed sequence tags (A1, A2, A4, A5, A6 and A11) were up-regulated at the early stage of infection. In this study, we cloned and characterized these transcripts. The full-length nucleic acid sequences of channel catfish annexins ranges from 1231 (annexin A1) to 2476 (annexin A6). Each transcript has one open reading, which appears to encode peptides ranges from 317 to 662 amino acid residues with the calculated molecular masses from 35.0 (annexin A5) to 74.5 kDa (annexin A6). Phylogenetic and sequence analysis demonstrates that each channel catfish annexin had a diversified amino terminus, and had four structurally conserved 70-amino-acid repeats. In addition, several important features for annexin functions were conserved in channel catfish. For expression profile, channel catfish annexin A1, A4 and A6 transcripts were detected in spleen, anterior kidney, liver, intestine, skin and gill of fish examined. However, annexin A2, A5 and A11 cDNAs were variously detected in tissues of fish sampled. This result provides important information for further elucidating channel catfish annexin functions in vivo.

Last Modified: 7/24/2014
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