Sotelo-Mundo Rogerio R, Islas-Osuna Maria A, de-la-Re-Vega Enrique, Hernández-López Jorge, Vargas-Albores Francisco, Yepiz-Plascencia Gloria
Aquatic Molecular Biology Laboratory, Centro de Investigación en Alimentación y Desarrollo, P.O. Box 1735, Hermosillo, Sonora 83000, Mexico.
Fish Shellfish Immunol. 2003 Oct;15(4):325-31. doi: 10.1016/s1050-4648(02)00176-6.
Lysozyme, an antibacterial protein, has been implicated in innate immunity in invertebrates, but its activity in shrimp remained to be determined. We cloned the white shrimp lysozyme cDNA using a PCR strategy and detected its activity in haemocytes using a lytic-zone assay against Micrococcus luteus. The cloning was based on a reported EST (dbEST BE18831). The deduced amino acid sequence resulted in 150 amino with 46% identity to hen egg white lysozyme. RT-PCR was used to detect lysozyme mRNA in haemocytes. Analysis of the amino acid sequence of the shrimp lysozyme showed that it belongs to the C-type family of lysozymes. Furthermore, the lysozyme amino acid sequence contained extra residues at its C-terminus, which are characteristic of marine invertebrates. This information will be useful in future studies on the molecular mechanisms of immunity in marine invertebrates.
溶菌酶是一种抗菌蛋白,在无脊椎动物的先天免疫中发挥作用,但其在虾类中的活性仍有待确定。我们采用PCR策略克隆了凡纳滨对虾溶菌酶cDNA,并通过针对藤黄微球菌的溶菌圈试验检测了其在血细胞中的活性。该克隆基于一条已报道的EST(dbEST BE18831)。推导的氨基酸序列有150个氨基酸,与鸡蛋白溶菌酶有46%的同源性。采用RT-PCR检测血细胞中溶菌酶mRNA。对虾溶菌酶氨基酸序列的分析表明,它属于C型溶菌酶家族。此外,溶菌酶氨基酸序列在其C末端含有额外的残基,这是海洋无脊椎动物的特征。这些信息将有助于未来对海洋无脊椎动物免疫分子机制的研究。