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Attacin gene sequence variations in different ecoraces of tasar silkworm Antheraea mylitta.

ABSTRACT: Attacin gene exists as paralogous conversion and is being used for identification of strain variations in insects based on the sequence variation. Hence, a study was undertaken to analyze the sequence variation of the attacin gene isoforms in the tasar silkworm Anthereae mylitta that exists in the form of different ecoraces depending upon the environment, food plant and location. Comparison of the previously reported attacin sequences with the DNA sequences of attacin A and B genes revealed six amino acid substitutions among the sequences of the ecoraces which however did not affect the functional domain of Attacin. The generated dendrogram clearly indicated unique branches for each ecorace with two separate gene clusters for attacin A and B. The Sarihan ecorace formed a separate sub-group under both the gene clusters. The present study also revealed the presence of Attacin_N Superfamily domain exclusively in Exon I separated from the Attacin_C Superfamily domain that was present in Exon II and part of Exon III, a prominent character of attacin gene. The phylogenetic reconstruction analysis of attacin gene in A.mylitta supported the common evolutionary origin of attacin genes belonging to the Lepidoteran and Dipteran families that formed two separate clusters.

SUBMITTER: Sudha R

PROVIDER: S-EPMC4658647 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

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Project description:BackgroundCocoonase is a serine protease present in sericigenous insects and majorly involved in dissolving of sericin protein allowing moth to escape. Cocoon structure is made up of sericin protein which holds fibroin filaments together. Cocoonase enzyme hydrolyzes sericin protein without harming the fibroin. However, until date, no detailed characterization of cocoonase enzyme and its presence in wild silk moth Antheraea mylitta has been carried out. Therefore, current study aimed for detailed characterization of amplified cocoonase enzyme, secondary and tertiary structure prediction, sequence and structural alignment, phylogenetic analysis, and computational validation. Several computational tools such as ProtParam, Iterative Threading Assembly Refinement (I-TASSER), PROCHECK, SAVES v6.0, TM-align, Molecular Evolutionary Genetics Analysis (MEGA) X, and Figtree were employed for characterization of cocoonase protein.ResultsThe present study elucidates about the isolation of RNA, cDNA preparation, PCR amplification, and in silico characterization of cocoonase from Antheraea mylitta. Here, total RNA was isolated from head region of A. mylitta, and gene-specific primers were designed using Primer3 followed by PCR-based amplification and sequencing. The newly constructed 377-bp length sequence of cocoonase was subjected to in silico characterization. In silico study of A. mylitta cocoonase showed 26% similarity to A. pernyi strain Qing-6 cocoonase using Blastp and belongs to member of chymotrypsin-like serine protease superfamily. From phylogenetic study, it was found that A. mylitta cocoonase sequence is closely related to A. pernyi cocoonase sequence.ConclusionsThe present study revealed about the detailed in silico characterization of cocoonase gene and encoded protein obtained from A. mylitta head region. The results obtained infer the presence of cocoonase enzyme in the wild silkworm A. mylitta and can be used for cocoon degumming which will be a valuable and cost-effective strategy in silk industry.

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Attacin gene sequence variations in different ecoraces of tasar silkworm Antheraea mylitta.

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