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

被引:5
作者
Chang, Yun-Shiang [1 ]
Chen, Jian-Nan [2 ]
Chang, Kun-Hung [1 ]
Chang, Yi-Ming [3 ]
Lai, Ying-Jang [4 ]
Liu, Wang-Jing [3 ]
机构
[1] Da Yeh Univ, Dept Mol Biotechnol, Changhua, Taiwan
[2] Natl Taiwan Univ, Inst Food Sci & Technol, Taipei, Taiwan
[3] Univ Taipei, Dept Earth & We Sci, 1 Ai Guo West Rd, Taipei 10048, Taiwan
[4] Natl Quemoy Univ, Dept Food Sci, Kinmen, Taiwan
关键词
WSSV; Lectin; Agrocybe aegerita; PENAEUS-MONODON; STRUCTURAL PROTEINS; HISTORIC EMERGENCE; PROTEOMIC ANALYSIS; EDIBLE MUSHROOMS; ANTITUMOR LECTIN; ENVELOPE; IDENTIFICATION; PURIFICATION; DISEASES;
D O I
10.1016/j.dci.2018.07.020
中图分类号
S9 [水产、渔业];
学科分类号
0908 ;
摘要
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 mu g/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.
引用
收藏
页码:1 / 9
页数:9
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