A single-CRD C-type lectin is important for bacterial clearance in the silkworm

Zhan, Ming-Yue; Toufeeq, Shahzad; Yang, Pei-Shan; Liu, Su; Yu, Xiao‐Qiang; Rao, Xiang‐Jun

doi:10.1016/j.dci.2016.08.004

Cited by 49 publications

(36 citation statements)

References 44 publications

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“…Furthermore, agglutination activity is a basic action for organisms to resist invading pathogens, and binding is the first step for this defence mechanism (Xu et al , ). In our carbohydrate binding assay, TcCTL6 bound LPS and PGN in a dose‐dependent manner, which is similar to the condition in which a CTL with a QPD motif from the silkworm could bind to different microbial cell wall components (Zhan et al , ). In the mosquito Armigeres subalbatus , five CTLs could bind to different polysaccharides, such as LPS, lipid A, PGN, lipoteichoic acid, zymosan and laminarin (Shi et al , ).…”

Section: Discussionsupporting

confidence: 72%

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

Feng

et al. 2019

Insect Molecular Biology

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C‐type lectins are one of the pattern‐recognition proteins involved in innate immunity in invertebrates. Although there are 16 C‐type lectin genes that have been identified in the genome of Tribolium castaneum, their functions and mechanisms in innate immunity remain unknown. Here, we identified one C‐type lectin orthologue, TcCTL6 (TC003708), by sequencing random clones from the cDNA library of the coleopteran beetle, T. castaneum. TcCTL6 contains a 654 bp open reading frame encoding a protein of 217 amino acids that includes a single carbohydrate‐recognition domain. The expression of TcCTL6 was significantly induced by Escherichia coli, Staphylococcus aureus and stimulation with carbohydrates, including lipopolysaccharide and peptidoglycan. A binding assay suggested that the recombinant TcCTL6 not only bound to lipopolysaccharide and peptidoglycan but also bound to Gram‐positive (S. aureus, Bacillus subtilis and Bacillus thuringiensis) and Gram‐negative bacteria (E. coli and Pseudomonas aeruginosa) in the presence of calcium ions. Furthermore, when TcCTL6 was knocked down by RNA interference, four antimicrobial peptides (attacin1, attacin2, coleoptericin1 and coleoptericin2) were significantly decreased. These results demonstrate that TcCTL6 plays a vital role in the immune response towards pathogen infection by influencing the expression of antimicrobial peptides and the agglutination of bacteria in the presence of calcium ions in T. castaneum.

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Section: Discussionsupporting

confidence: 72%

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

Feng

et al. 2019

Insect Molecular Biology

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“…These three clades were in turn part of a single branch in the phylogenetic tree which was distant from other major branches, and were characterized as “CTL‐S” type (single‐CRD) (Rao et al ., ). CTL‐S has more diversified functions in development and immunity, which involves defense against Gram‐negative bacteria, requiring the development of the trachea system and bacteria clearance (Rao et al ., ; Zhan et al ., ). Bm CTL5 (CTL‐S3) is known to function as an opsonin in larval hemolymph to enhance the clearance of pathogens (Zhan et al ., ).…”

Section: Resultsmentioning

confidence: 97%

“…CTL‐S has more diversified functions in development and immunity, which involves defense against Gram‐negative bacteria, requiring the development of the trachea system and bacteria clearance (Rao et al ., ; Zhan et al ., ). Bm CTL5 (CTL‐S3) is known to function as an opsonin in larval hemolymph to enhance the clearance of pathogens (Zhan et al ., ). The presence of 1 : 1 orthologs between Bm CTL5 and Ma CTL13 (Fig.…”

Section: Resultsmentioning

confidence: 97%

Comparative analysis of the Monochamus alternatus immune system

Zhou

Zhang

et al. 2017

Insect Science

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The pine sawyer beetle, Monochamus alternatus, is regarded as a notorious forest pest in Asia, vectoring an invasive pathogenic nematode, Bursaphelenchus xylophilus, which is known to cause pine wilt disease. However, little sequence information is available for this vector beetle. This hampered the research on its immune system. Based on the transcriptome of M. alternatus, we have identified and characterized 194 immunity-related genes in M. alternatus, and compared them with homologues molecules from other species known to exhibit immune responses against invading microbes. The lower number of putative immunity-related genes in M. alternatus were attributed to fewer C-type lectin, serine protease (SP) and anti-microbial peptide (AMP) genes. Phylogenetic analysis revealed that M. alternatus had a unique recognition gene, galectin3, orthologues of which were not identified in Tribolium castaneum, Drosophila melanogastor, Anopheles gambiae and Apis mellifera. This suggested a lineage-specific gene evolution for coleopteran insects. Our study provides the comprehensive sequence resources of the immunity-related genes of M. alternatus, presenting valuable information for better understanding of the molecular mechanism of innate immunity processes in M. alternatus against B. xylophilus.

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“…Samples were then subjected to western blot analysis. Binding of PGRP-S4 to immobilized peptidoglycans were analysed by a plate ELISA assay as described previously (Zhan et al, 2016). Briefly, peptidoglycans from E. coli K12, B. subtilis and St. aureus were diluted to 40 lg/ml with pyrogen-free water.…”

Section: Binding Of Pgrp-s4 To Bacteria and Peptidoglycansmentioning

confidence: 99%

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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A single-CRD C-type lectin is important for bacterial clearance in the silkworm

Cited by 49 publications

References 44 publications

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

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

Comparative analysis of the Monochamus alternatus immune system

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

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