The lectin domain containing proteins with mucosal immunity and digestive functions in oyster Crassostrea gigas. Issue 89 (June 2019)

• Record Type: Journal Article
• Authors: Wang, Weilin; Gong, Changhao; Han, Zirong; Lv, Xiaojing; Liu, Shujing; Wang, Lingling; Song, Linsheng
• Is Part Of: Fish & shellfish immunology. Issue 89(2019)
• Page Start: 237
• Page End: 247
• Publication Date: 2019-06
• Subjects: Crassostrea gigas -- Lectin domain -- C-type lectin -- Mucosal immunity -- Digestive functions; Fishes -- Immunology -- Periodicals; Shellfish -- Immunology -- Periodicals; Poissons -- Immunologie -- Périodiques; Crustacés -- Immunologie -- Périodiques; 571.9617
• DOI: 10.1016/j.fsi.2019.03.067
• Languages: English
• ISSNs: 1050-4648

Abstract

Abstract: Lectins are carbohydrate-binding proteins with lectin domains, which are extensively studied for their numerous roles in biological recognition. However, the lectin domain containing proteins (LDCPs) chimerized with other non-lectin domains have not received sufficient attention. In the present study, a genome-wide survey of LDCPs in oyster Crassostrea gigas was conducted, and an expansive 640 LDCPs derived from ten lectin domains were identified and functionally explored. In these LDCPs, a total of 282 kinds of domains were predicted, and 90% of the LDCPs contained more than one kind of domain. The lectin domains were frequently fused with non-lectin domains, such as epidermal growth factor domain and peptidase related domains, which supplied LDCPs with more diversity in structures and functions. The C-type lectin domains were the most abundant domains in LDCPs, and they were largely co-existed with non-lectin domains of complement activation-related domains (such as CUB domain and PAN-1 domain) but relative independence with other lectin domains. Furthermore, the C-type lectin domain containing proteins (CTLPs) found to mainly act as pattern immune recognition receptors and were highly expressed in mucosal tissues (digestive gland, male gonad and labial palp) to provide mucosal immune protections. The Concanavalin A-like lectin domains were the second richest domains in LDCPs, and they were mostly constructed into chimeric proteins with epidermal growth factor domain and peptidase related domains. The Concanavalin A-like lectin domain containing proteins (CALPs) were significantly enriched with peptidase activities and mainly expressed in digestive tissues. All the results suggested the mucosal immunity and digestive functions of oyster LDCPs, which provided a fresh idea about the functions of invertebrate lectin family. Highlights: The 640 LDCPs derived from ten lectin domains were identified in oyster Crassostrea gigas. The non-lectin domains supplied LDCPs with more diversification of structure and function. The CTLPs mainly functioned as pattern recognition receptors in mucosal tissues. The Concanavalin A-like lectin domain fused with peptidase mainly expressed in digestive tissues.