Structural features, evolutionary relationships, and transcriptional regulation of C-type lectin-domain proteins in Manduca sexta.
Structural features, evolutionary relationships, and transcriptional regulation of C-type lectin-domain proteins in Manduca sexta.
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DOI:
10.1016/j.ibmb.2014.12.006
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发表时间:
2015-07
影响因子:
3.8
通讯作者:
Jiang, Haobo
中科院分区:
文献类型:
--
作者:
Rao, Xiang-Jun;Cao, Xiaolong;He, Yan;Hu, Yingxia;Zhang, Xiufeng;Chen, Yun-Ru;Blissard, Gary;Kanost, Michael R.;Yu, Xiao-Qiang;Jiang, Haobo
关键词:
C-type lectins (CTLs) are a large family of Ca2+-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 Ca2+-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.
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