Comparative analysis of C‐type lectin domain proteins in the ghost moth, Thitarodes xiaojinensis (Lepidoptera: Hepialidae)

Abstract

Insects have a large family of C-type lectins involved in cell adhesion, pathogen recognition and activation of immune responses. In this study, 32 transcripts encoding C-type lectin domain proteins (CTLDPs) were identified from the Thitarodes xiaojinensis transcriptome. According to their domain structures, six CTLDPs with one carbohydrate-recognition domain (CRD) were classified into the CTL-S subfamily. The other 23 CTLDPs with two CRDs were grouped into the immulectin (IML) subfamily. The remaining three with extra regulatory domains were sorted into the CTL-X subfamily. Phylogenetic analysis showed that CTL-S and CTL-X members from different insects could form orthologous groups. In contrast, no T. xiaojinensis IML orthologues were found in other insects. Remarkable lineage-specific expansion in this subfamily was observed reflecting that these CTLDPs, as important receptors, have evolved diversified members in response to a variety of microbes. Prediction of binding ligands revealed that T. xiaojinensis, a cold-adapted species, conserved the ability of CRDs to combine with Ca to keep its receptors from freezing. Comparative analysis of induction of CTLDP genes after different immune challenges indicated that IMLs might play critical roles in immune defenses. This study examined T. xiaojinensis CTLDPs and provides a basis for further studies of their characteristics.

A C‐type lectin with a single carbohydrate‐recognition domain involved in the innate immune response of Tribolium castaneum

“…Our phylogenetic analysis indicated that AgCTLGA , DmCG4115 and TcCTL6 formed one orthologous group. BmCTLS2 and BmCTLS3 were located closely in other sister subbranches (Meng et al , ). Moreover, amino acid sequence alignment analysis found that the orthologues possessed high sequence similarity and many common structural features, suggesting that they have similar functions.…”

“…One of the five branches has three sister subbranches. The characteristics of two sister subbranches represented by BmCTLS2 and BmCTLS3 have been studied, whereas the functions of the other branch where TcCTL6 is located have not been studied (Meng et al , ). In this study, TcCTL6 was cloned for the first time from T. castaneum , and its role in immune defence in response to bacterial challenge was also investigated.…”

Immune-related genes of the larval Holotrichia parallela in response to entomopathogenic nematodes Heterorhabditis beicherriana LF

“…Identi cation of parasite/pathogen invasion in the host is the initial step in the initiation of immune responses, and this process relies on biosensor proteins called pattern recognition receptors (PRRs), which can detect and bind to certain pathogen-associated molecular patterns (PAMPs) on the surface of invading microbes or foreign bodies [52,53]. PGRPs are important members of insect PRRs and play an important role in innate immunity [54,55].…”

Proteomic Responses Under Cold Stress Reveal Unique Cold Tolerance Mechanisms in the Pacific White Shrimp (Litopenaeus vannamei)

“…On the structural level, the lectin protein family is tightly related to cold tolerance ( Moulessehoul et al, 1992 ; Gronwald et al, 1998 ). Interestingly, the function of lectin proteins relies on alpha1,3-galactosyltransferase ( Khraltsova et al, 2000 ), cytoskeleton ( Timofeeva et al, 2000 ), and especially rely on the lectin type ( Meng et al, 2017 ; Hung et al, 2018 ). In this study, three C-type lectin proteins were differentially expressed under the different temperature treatments (Figure 5 ), suggesting that each individual lectin played a specific role in cold tolerance in this organism.…”