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首页> 外文期刊>The FEBS journal >Comprehensive sequence analysis of horseshoe crab cuticular proteins and their involvement in transglutaminase-dependent cross-linking
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Comprehensive sequence analysis of horseshoe crab cuticular proteins and their involvement in transglutaminase-dependent cross-linking

机译：crab蟹表皮蛋白的全面序列分析及其参与转谷氨酰胺酶依赖性交联的过程

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摘要

Arthropod cuticles play an important role as the first barrier against invading pathogens. We extensively determined the sequences of horseshoe crab cuticular proteins. Proteins extracted from a part of the ventral side of the cuticle were purified by chitin-affinity chromatography, and separated by two-dimensional SDS/PAGE. Proteins appearing on the gel were designated high molecular mass chitin-binding proteins, and these proteins were then grouped into classes based on their approximate isoelectric points and predominant amino acid compositions. Members of groups designated basic G, basic Y, and acidic S groups contained a so-called Rebers and Riddiford consensus found in arthropod cuticular proteins. Proteins designated acidic DE25 and DE29 each contained a Cys-rich domain with sequences similar to those of insect peritrophic matrix proteins and chitinases. In contrast, basic QH4 and QH10 contained no consensus sequences found in known chitin-binding proteins. Alternatively, a low molecular mass chitin-binding fraction was prepared by size exclusion chromatography, and 15 low molecular mass chitin-binding proteins, named P1 through P15, were isolated. With the exception of P9 and P15, all were found to be identical to known antimicrobial peptides. P9 consisted of a Kunitz-type chymotrypsin inhibitor sequence, and P15 contained a Cys-rich motif found in insulin-like growth factor-binding proteins. Interestingly, we observed transglutaminase-dependent polymerization of nearly all high molecular mass chitin-binding proteins, a finding suggests that transglutaminase-dependent cross-linking plays an important role in host defense in the arthropod cuticle, analogous to that observed in the epidermal cornified cell envelope in mammals.
机译：节肢动物角质层作为入侵病原体的第一道屏障发挥着重要作用。我们广泛地确定了crab的表皮蛋白的序列。通过几丁质亲和层析纯化从表皮的腹侧的一部分提取的蛋白质，并通过二维SDS / PAGE分离。出现在凝胶上的蛋白质称为高分子几丁质结合蛋白，然后根据它们的近似等电点和主要氨基酸组成将这些蛋白质分为几类。命名为碱性G，碱性Y和酸性S基团的成员包含在节肢动物表皮蛋白中发现的所谓的Rebers和Riddiford共识。命名为酸性DE25和DE29的蛋白质各包含一个富含Cys的结构域，其序列与昆虫营养丰富的基质蛋白和几丁质酶相似。相反，基本的QH4和QH10不包含在已知几丁质结合蛋白中发现的共有序列。或者，通过尺寸排阻色谱法制备低分子量的几丁质结合蛋白部分，并分离出15种低分子量的几丁质结合蛋白，命名为P1至P15。除P9和P15外，均与已知的抗菌肽相同。 P9由Kunitz型胰凝乳蛋白酶抑制剂序列组成，P15包含在胰岛素样生长因子结合蛋白中发现的富含Cys的基序。有趣的是，我们观察到几乎所有高分子几丁质结合蛋白都依赖转谷氨酰胺酶聚合，这一发现表明，与表皮角质化细胞中观察到的相似，转谷氨酰胺酶依赖的交联在节肢动物表皮的宿主防御中起着重要作用。哺乳动物的信封。

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