Cloning and expression of the lectin gene from the mushroom Agrocybe aegerita and the activities of recombinant lectin in the resistance of shrimp white spot syndrome virus infection

Lectin is a protein with multiple functions. In this study, the full-length cDNA of the Agrocybe aegerita lectin (AAL) gene was cloned, recombinant AAL (AAL-His) was expressed, and the activities of AAL-His were analyzed. Northern blot analysis showed that the major AAL transcript is approximately 9...

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Veröffentlicht in:Developmental and comparative immunology 2019-01, Vol.90, p.1-9
Hauptverfasser: Chang, Yun-Shiang, Chen, Jian-Nan, Chang, Kun-Hung, Chang, Yi-Ming, Lai, Ying-Jang, Liu, Wang-Jing
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Sprache:eng
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Zusammenfassung:Lectin is a protein with multiple functions. In this study, the full-length cDNA of the Agrocybe aegerita lectin (AAL) gene was cloned, recombinant AAL (AAL-His) was expressed, and the activities of AAL-His were analyzed. Northern blot analysis showed that the major AAL transcript is approximately 900 bp. Sequence analysis showed that the coding region of AAL is 489 bp with a transcription start site located 39 nucleotides upstream of the translation initiation codon. In an agglutination test, AAL-His agglutinated rabbit erythrocytes at 12.5 μg/ml. AAL-His also showed antiviral activity in protecting shrimp from white spot syndrome virus (WSSV) infection. This anti-WSSV effect might be due to the binding of AAL-His on WSSV virions via the direct interactions with four WSSV structural proteins, VP39B, VP41B, VP53A and VP216. AAL demonstrates the potential for development as an anti-WSSV agent for shrimp culture. It also implies that these four AAL interaction WSSV proteins may play important roles in virus infection. •Full length cDNA of Agrocybe aegerita lectin (AAL) gene was cloned.•Recombinant AAL (AAL-His) showed with anti- white spot syndrome virus (WSSV) activity.•The anti-WSSV effect of AAL-His might through to its binding on WSSV virions.•AAL-His could interact with WSSV structural proteins, VP39B, VP41B, VP53A and VP216.
ISSN:0145-305X
1879-0089
DOI:10.1016/j.dci.2018.07.020