Cloning, expression and phylogenetic analysis of Hemolin, from the Chinese oak silkmoth, Antheraea pernyi.
The Chinese oak silk moth Antheraea pernyi is an important silk producer. To understand microbial resistance of this moth, we cloned Hemolin, encoding a multifunctional immune protein belonging to the immunoglobulin superfamily, and examined the expression in gonads and fat body. The ApHemolin amino acid sequence was compared to other Hemolin sequences in order to predict functional sites. Several sites were conserved; among them a phosphate binding site, which according to 3D structure modelling does not appear in neuroglian, the phylogenetically closest related protein. In addition, two conserved KDG sequences in the C-C' loop of immunoglobulin domains 1 and 3, give rise to gamma-turns, which is a common motif in the C'-C'' loop of the hypervariable region L2 in vertebrate immunoglobulins. The comparisons also show variable regions of specific interest for future studies of hemolin and its interaction with microbial entities.
Department of Genetics, Microbiology and Toxicology, Stockholm University, Svante Arrheniuse v. 16E, SE-106 91 Stockholm, Sweden.
Wenli
W
Li
Olle
O
Terenius
Makoto
M
Hirai
Anders S
AS
Nilsson
Ingrid
I
Faye
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D017124:Conserved Sequence; D018076:DNA, Complementary / Q000235:genetics; D005260:Female; D015870:Gene Expression; D017344:Genes, Insect; D007136:Immunoglobulins / Q000235:genetics*; D019476:Insect Proteins / Q000235:genetics*; D008297:Male; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009036:Moths / Q000235:genetics* / Q000276:immunology*; D010802:Phylogeny; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D007136:Immunoglobulins; D019476:Insect Proteins; C066846:hemolin