Molecular cloning and characterization of a T24-like protein in Echinococcus multilocularis.
One tetraspanin, designated as E24, was cloned from a full-length enriched vector-capping cDNA library of Echinococcus multilocularis metacestode. The amino acid sequence and phylogenetic analysis suggested that E24 is a T24-like protein. The crucial, functional large extracellular loop (LEL) domain of E24 was expressed and characterized using a polyclonal antiserum by Western blot and immunohistochemistry. The results showed that anti-recombinant-E24 (anti-recE24) antibody can specifically recognize approximately 25 kDa recombinant protein and 25 kDa cyst-extracted antigen; the germinal layer of both the protoscolex-free and protoscolex-formed cysts were intensely labeled by immunofluorescent antibody. This study revealed that E24 is an antigenic, germinal layer-located protein of E. multilocularis metacestode, implying for its potential in diagnostic and vaccine development.
Dang
Zhisheng
Z
Department of Collaboration and Education, Research Center for Zoonosis Control, Hokkaido University, Sapporo, Japan.
Watanabe
Junichi
J
Kajino
Kiichi
K
Oku
Yuzaburo
Y
Matsumoto
Jun
J
Yagi
Kinpei
K
Kouguchi
Hirokazu
H
Sugimoto
Chihiro
C
D000818:Animals; D000909:Antibodies, Helminth / Q000276:immunology; D000947:Antigens, Helminth / Q000235:genetics* / Q000276:immunology; D015153:Blotting, Western; D002462:Cell Membrane / Q000737:chemistry; D003001:Cloning, Molecular; D016000:Cluster Analysis; D018509:DNA, Helminth / Q000737:chemistry / Q000235:genetics; D048210:Echinococcus multilocularis / Q000737:chemistry / Q000235:genetics*; D015801:Helminth Proteins / Q000235:genetics* / Q000276:immunology; D008856:Microscopy, Fluorescence; D008969:Molecular Sequence Data; D010802:Phylogeny; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid
D000909:Antibodies, Helminth; D000947:Antigens, Helminth; D018509:DNA, Helminth; D015801:Helminth Proteins