Identification of C-type lectin-domain proteins (CTLDPs) in silkworm Bombyx mori

Rao, Xiang‐Jun; Toufeeq, Shahzad; Liu, Su; Wu, Peng; Yang, He; Sun, Weijia; Fan, Xiangyun; Yang, Yunfan; Shi, Qiao; Yu, Xiao‐Qiang

doi:10.1016/j.dci.2015.07.005

Cited by 56 publications

(50 citation statements)

References 57 publications

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“…In addition, T. xiaojinensis CTL‐S1 through S6 reveal monophyletic groups with their orthologues from other insects. In M. sexta and B. mori , three IMLs possess their own 1 : 1 orthologues (Rao et al ., , b). However, orthologous pairs of all identified T. xiaojinensis IMLs could not be detected.…”

Section: Resultsmentioning

confidence: 99%

“…C‐type lectin domain protein amino acid sequences from M. sexta , B. mori and A. aegypti (Shin et al ., ; Rao et al ., , b; Wang et al ., ) were accessed as queries to search the T. xiaojinensis unigene database (Meng et al ., ). In total, 32 transcripts were confirmed by sequencing and deposited in the GenBank database (Table S3).…”

Section: Methodsmentioning

confidence: 99%

“…However, evidence shows that not all C‐type lectins have the ability to associate with carbohydrates or Ca 2+ (Zelensky & Gready, ). We therefore employed annotation studies in Manduca sexta and Bombyx mori to use C‐type lectin domain proteins (CTLDPs) to refer to proteins harboring the domains (Rao et al ., , b).…”

Section: Introductionmentioning

confidence: 99%

“…In Lepidoptera, the number of CTLDs in CTLDPs is distinctive. Besides the proteins present in one CTLD, there are also extraordinary CTLDPs possessing dual and triple CTLDs (Rao et al ., , b). CTLDPs with two CTLDs are also found in T. castaneum (Zou et al ., ).…”

Section: Introductionmentioning

confidence: 99%

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

Meng

Zhang

et al. 2018

Insect Science

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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.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

Meng

Zhang

et al. 2018

Insect Science

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“…For example, Drosophila PGRP‐LC has three splicing variants (–LCx, ‐LCa and –LCy) that carry out different functions alone or in cooperation with other PGRPs (Pal & Wu, ; Royet et al ., ). Remarkably, mammalian PGLYRP3/4 and Drosophila PGRP‐LF have tandem dual PGRP domains, reminiscent of the single and dual carbohydrate recognition domain lectins (Rao et al ., 2015a, b, 2016). Four of the six B. mori PGRP‐S (‐S1,‐S2,‐S3 and ‐S5) have been characterized.…”

Section: Discussionmentioning

confidence: 97%

Molecular cloning and characterization of a short peptidoglycan recognition protein from silkworm Bombyx mori

Yang

Zhan

et al. 2017

Insect Molecular Biology

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Peptidoglycan is the major bacterial component recognized by the insect immune system. Peptidoglycan recognition proteins (PGRPs) are a family of pattern-recognition receptors that recognize peptidoglycans and modulate innate immune responses. Some PGRPs retain N-acetylmuramoyl-L-alanine amidase (Enzyme Commission number: 3.5.1.28) activity to hydrolyse bacterial peptidoglycans. Others have lost the enzymatic activity and work only as immune receptors. They are all important modulators for innate immunity. Here, we report the cloning and functional analysis of PGRP-S4, a short-form PGRP from the domesticated silkworm, Bombyx mori. The PGRP-S4 gene encodes a protein of 199 amino acids with a signal peptide and a PGRP domain. PGRP-S4 was expressed in the fat body, haemocytes and midgut. Its expression level was significantly induced by bacterial challenges in the midgut. The recombinant PGRP-S4 bound bacteria and different peptidoglycans. In addition, it inhibited bacterial growth and hydrolysed an Escherichia coli peptidoglycan in the presence of Zn . Scanning electron microscopy showed that PGRP-S4 disrupted the bacterial cell surface. PGRP-S4 further increased prophenoloxidase activation caused by peptidoglycans. Taken together, our data suggest that B. mori PGRP-S4 has multiple functions in immunity.

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Molecular cloning and analysis of a C‐type lectin from silkworm Bombyx mori

Toufeeq

Zhan

Yang

et al. 2017

Arch Insect Biochem Physiol

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C-type lectins (CTLs) play a variety of roles in plants and animals. They are involved in animal development, pathogen recognition, and the activation of immune responses. CTLs carry one or more non-catalytic carbohydrate-recognition domains (CRDs) to bind specific carbohydrates reversibly. Here, we report the molecular cloning and functional analysis of a single-CRD CTL, named C-type lectin-S2 (BmCTL-S2) from the domesticated silkmoth Bombyx mori (Lepidoptera: Bombycidae). The ORF of CTL-S2 is 666 bp, which encodes a putative protein of 221 amino acids. BmCTL-S2 is expressed in a variety of immune-related tissues, including hemocytes and fat body among others. BmCTL-S2 mRNA level in the midgut and the fat body was significantly increased by bacterial challenges. The recombinant protein (rBmCTL-S2) bound different bacterial cell wall components and bacterial cells. rBmCTL-S2 also inhibited the growth of Bacillus subtilis and Staphylococcus aureus. Taken together, we infer that BmCTL-S2 is a pattern-recognition receptor with antibacterial activities.

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Identification of C-type lectin-domain proteins (CTLDPs) in silkworm Bombyx mori

Cited by 56 publications

References 57 publications

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

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

Molecular cloning and characterization of a short peptidoglycan recognition protein from silkworm Bombyx mori

Molecular cloning and analysis of a C‐type lectin from silkworm Bombyx mori

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