Structural features, evolutionary relationships, and transcriptional regulation of C-type lectin-domain proteins in Manduca sexta. (July 2015)
- Record Type:
- Journal Article
- Title:
- Structural features, evolutionary relationships, and transcriptional regulation of C-type lectin-domain proteins in Manduca sexta. (July 2015)
- Main Title:
- Structural features, evolutionary relationships, and transcriptional regulation of C-type lectin-domain proteins in Manduca sexta
- Authors:
- Rao, Xiang-Jun
Cao, Xiaolong
He, Yan
Hu, Yingxia
Zhang, Xiufeng
Chen, Yun-Ru
Blissard, Gary
Kanost, Michael R.
Yu, Xiao-Qiang
Jiang, Haobo - Abstract:
- Abstract: C-type lectins (CTLs) are a large family of Ca 2+ -dependent carbohydrate-binding proteins recognizing various glycoconjugates and functioning primarily in immunity and cell adhesion. We have identified 34 CTLDP (for CTL-domain protein) genes in the Manduca sexta genome, which encode proteins with one to three CTL domains. CTL-S1 through S9 (S for simple) have one or three CTL domains; immulectin-1 through 19 have two CTL domains; CTL-X1 through X6 (X for complex) have one or two CTL domains along with other structural modules. Nine simple CTLs and seventeen immulectins have a signal peptide and are likely extracellular. Five complex CTLs have both an N-terminal signal peptide and a C-terminal transmembrane region, indicating that they are membrane anchored. Immulectins exist broadly in Lepidoptera and lineage-specific gene duplications have generated three clusters of fourteen genes in the M. sexta genome, thirteen of which have similar expression patterns. In contrast to the family expansion, CTL-S1∼S6, S8, and X1∼X6 have 1:1 orthologs in at least four lepidopteran/dipteran/coleopteran species, suggestive of conserved functions in a wide range of holometabolous insects. Structural modeling suggests the key residues for Ca 2+ -dependent or independent binding of certain carbohydrates by CTL domains. Promoter analysis identified putative κB motifs in eighteen of the CTL genes, which did not have a strong correlation with immune inducibility in the mRNA or proteinAbstract: C-type lectins (CTLs) are a large family of Ca 2+ -dependent carbohydrate-binding proteins recognizing various glycoconjugates and functioning primarily in immunity and cell adhesion. We have identified 34 CTLDP (for CTL-domain protein) genes in the Manduca sexta genome, which encode proteins with one to three CTL domains. CTL-S1 through S9 (S for simple) have one or three CTL domains; immulectin-1 through 19 have two CTL domains; CTL-X1 through X6 (X for complex) have one or two CTL domains along with other structural modules. Nine simple CTLs and seventeen immulectins have a signal peptide and are likely extracellular. Five complex CTLs have both an N-terminal signal peptide and a C-terminal transmembrane region, indicating that they are membrane anchored. Immulectins exist broadly in Lepidoptera and lineage-specific gene duplications have generated three clusters of fourteen genes in the M. sexta genome, thirteen of which have similar expression patterns. In contrast to the family expansion, CTL-S1∼S6, S8, and X1∼X6 have 1:1 orthologs in at least four lepidopteran/dipteran/coleopteran species, suggestive of conserved functions in a wide range of holometabolous insects. Structural modeling suggests the key residues for Ca 2+ -dependent or independent binding of certain carbohydrates by CTL domains. Promoter analysis identified putative κB motifs in eighteen of the CTL genes, which did not have a strong correlation with immune inducibility in the mRNA or protein levels. Together, the gene identification, sequence comparisons, structure modeling, phylogenetic analysis, and expression profiling establish a solid foundation for future studies of M. sexta CTL-domain proteins. Graphical abstract: Highlights: Identified 9 simple and 6 complex CTL-domain proteins and 19 immulectins. Analyzed their structural features, evolution dynamics, and expression profiles. Modeled 56 CTL domains to predict their carbohydrate binding capability and specificity. … (more)
- Is Part Of:
- Insect biochemistry and molecular biology. Volume 62(2015:Jul.)
- Journal:
- Insect biochemistry and molecular biology
- Issue:
- Volume 62(2015:Jul.)
- Issue Display:
- Volume 62 (2015)
- Year:
- 2015
- Volume:
- 62
- Issue Sort Value:
- 2015-0062-0000-0000
- Page Start:
- 75
- Page End:
- 85
- Publication Date:
- 2015-07
- Subjects:
- Insect immunity -- Pattern recognition -- Carbohydrate recognition domain -- Expression profiling -- Comparative genomics
CTL C-type lectin -- CRD carbohydrate recognition domain -- CTLDP CTL-domain protein -- IML immulectin -- LC low complexity -- proPO prophenoloxidase -- MBL rat mannose binding lectin -- FPKM fragments per kilobase of exon per million fragments mapped -- C control -- I induced -- F fat body -- H hemocytes -- TM transmembrane -- SR scavenger receptor
Insect biochemistry -- Periodicals
Insects -- Physiology -- Periodicals
Insects -- Molecular aspects -- Periodicals
Biochemistry -- Periodicals
Insectes -- Biochimie -- Périodiques
Insectes -- Composition -- Périodiques
Insectes -- Physiologie -- Périodiques
Insectes -- Aspect moléculaire -- Périodiques
Biochimie -- Périodiques
Biochemistry
Insect biochemistry
Insects -- Molecular aspects
Insects -- Physiology
Periodicals
572.8157 - Journal URLs:
- http://www.sciencedirect.com/science/journal/09651748 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.ibmb.2014.12.006 ↗
- Languages:
- English
- ISSNs:
- 0965-1748
- Deposit Type:
- Legaldeposit
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- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4516.852000
British Library DSC - BLDSS-3PM
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- 2421.xml