The peptidoglycan recognition proteins (PGRPs).
The peptidoglycan recognition proteins (PGRPs).
复制标题
肽聚糖识别蛋白（PGRP）。
DOI：
10.1186/gb-2006-7-8-232
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发表时间：
2006
期刊：
影响因子：
12.3
通讯作者：
Gupta, Dipika
中科院分区：
文献类型：
--
作者：
Dziarski, Roman;Gupta, Dipika
肽聚糖识别蛋白（PGRP）存在于昆虫、软体动物、棘皮动物和脊椎动物中，它们保护动物免受感染。这四个哺乳动物家族成员是杀菌蛋白或水解细菌肽聚糖的酰胺酶。肽聚糖识别蛋白（PGRP）是存在于昆虫、软体动物、棘皮动物和脊椎动物中的天然免疫分子，但不存在于线虫和植物中。PGRP具有至少一个羧基末端PGRP结构域（约165个氨基酸长），其与噬菌体和细菌2型酰胺酶同源。昆虫有多达19个PGRP，分为短（S）和长（L）形式。短型存在于血淋巴、角质层和脂肪体细胞中，有时存在于肠的表皮细胞和血细胞中，而长型主要在血细胞中表达。昆虫PGRP的表达通常通过暴露于细菌而上调。昆虫PGRP激活Toll或免疫缺陷（Imd）信号转导途径或诱导蛋白水解级联反应，产生抗微生物产物，诱导吞噬作用，水解肽聚糖，并保护昆虫免受感染。哺乳动物有四种PGRP，它们是分泌的;目前尚不清楚是否有任何直接与昆虫PGRP直接相关。一种哺乳动物PGRP（PGLYRP-2）是N-乙酰胞壁酰-L-丙氨酸酰胺酶，其水解细菌肽聚糖并降低其促炎活性; PGLYRP-2从肝脏分泌到血液中，并且也由上皮细胞中的细菌诱导。其余三种哺乳动物PGRP是作为二硫键连接的同源和异源二聚体分泌的杀菌蛋白。PGLYRP-1主要在多形核白细胞颗粒中表达，PGLYRP-3和PGLYRP-4在皮肤、眼睛、唾液腺、咽喉、舌、食道、胃和肠中表达。这三种蛋白质通过与细胞壁肽聚糖相互作用来杀死细菌，而不是像其他抗菌肽那样渗透细菌膜。这些PGRP的直接杀菌活性要么在脊椎动物（或哺乳动物）谱系中进化，要么尚未在昆虫中发现。
Peptidoglycan recognition proteins (PGRPs) are found in insects, mollusks, echinoderms, and vertebrates, and they protect animals against infections. The four mammalian family members are either bactericidal proteins or amidases that hydrolyze bacterial peptidoglycan. Peptidoglycan recognition proteins (PGRPs) are innate immunity molecules present in insects, mollusks, echinoderms, and vertebrates, but not in nematodes or plants. PGRPs have at least one carboxy-terminal PGRP domain (approximately 165 amino acids long), which is homologous to bacteriophage and bacterial type 2 amidases. Insects have up to 19 PGRPs, classified into short (S) and long (L) forms. The short forms are present in the hemolymph, cuticle, and fat-body cells, and sometimes in epidermal cells in the gut and hemocytes, whereas the long forms are mainly expressed in hemocytes. The expression of insect PGRPs is often upregulated by exposure to bacteria. Insect PGRPs activate the Toll or immune deficiency (Imd) signal transduction pathways or induce proteolytic cascades that generate antimicrobial products, induce phagocytosis, hydrolyze peptidoglycan, and protect insects against infections. Mammals have four PGRPs, which are secreted; it is not clear whether any are directly orthologous to the insect PGRPs. One mammalian PGRP, PGLYRP-2, is an N-acetylmuramoyl-L-alanine amidase that hydrolyzes bacterial peptidoglycan and reduces its proinflammatory activity; PGLYRP-2 is secreted from the liver into the blood and is also induced by bacteria in epithelial cells. The three remaining mammalian PGRPs are bactericidal proteins that are secreted as disulfide-linked homo- and hetero-dimers. PGLYRP-1 is expressed primarily in polymorphonuclear leukocyte granules and PGLYRP-3 and PGLYRP-4 are expressed in the skin, eyes, salivary glands, throat, tongue, esophagus, stomach, and intestine. These three proteins kill bacteria by interacting with cell wall peptidoglycan, rather than permeabilizing bacterial membranes as other antibacterial peptides do. Direct bactericidal activity of these PGRPs either evolved in the vertebrate (or mammalian) lineage or is yet to be discovered in insects.
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影响因子：
6.7
作者：
Bischoff V;Vignal C;Duvic B;Boneca IG;Hoffmann JA;Royet J
通讯作者：
Royet J
影响因子：
20.3
作者：
Cho, JH;Fraser, IP;Ezekowitz, RAB
通讯作者：
Ezekowitz, RAB
DOI：
10.1073/pnas.0404952102
发表时间：
2005-01-25
影响因子：
11.1
作者：
Choe, KM;Lee, H;Anderson, KV
通讯作者：
Anderson, KV
影响因子：
3.6
作者：
Dziarski, R
通讯作者：
Dziarski, R
影响因子：
5.6
作者：
Guan, RJ;Wang, Q;Mariuzza, RA
通讯作者：
Mariuzza, RA