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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2021.12
- 수록면
- 1,497 - 1,502 (6page)
- DOI
- 10.1007/s13258-021-01183-z
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초록· 키워드
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Background Chitinase is a multi-functional enzyme that catalyzes the hydrolysis of β-1,4-linkages between N-acetylglucosamines (GlcNAc) in chitin. Recent studies imply that earthworm chitinase is implicated in self-defense immunity against chitin-containing pathogens. However, a direct relationship of earthworm chitinase with innate immunity has not yet been established.
Objective In this study, earthworm (Eisenia andrei) chitinase expression was examined following bacterial challenge by Bacillus subtilis.
Methods RNA sequencing (RNA-seq) and real-time quantitative reverse transcription polymerase chain reaction (qRT-PCR) were used to quantitatively evaluate mRNA expression changes in response to bacterial stimulation.
Results Multiple chitinase-related mRNAs were found to be upregulated, among which EaChi3, EaChi4, and EaChi2 were upregulated by approximately eightfold, eightfold, and 2.5-fold, respectively. This strongly suggested that earthworm chitinases may act as inducible humoral efectors in earthworm innate immunity. The primary structures of all three chitinases contained an N-terminal glycol_18 domain with two chitin-binding and chitin-catalyzing domains, and a C-terminal proline, glycine, serine, threonine (PGST)-rich domain. In addition, EaChi2 had a chitin-binding peritrophin-A domain at the end of the C-terminus with 5 cysteine residues possibly contributing two intradomain disulfde bonds. Multiple sequence alignment of the catalytic domain centers of glycol_18 domain displayed highly conserved chitin-binding and chitin-catalyzing domains in which three essential amino acid residues (D, D, E) for catalyzing activity are well conserved except EaChi4. The critical glutamic acid (E) residue was substituted for glutamine (Q) in EaChi4 indicating that it is devoid of catalytic activity.
Conclusions To our knowledge, this is the frst report providing direct evidence that multiple earthworm chitinases are bacteria-responsive, strongly suggesting that earthworm chitinases are inducible humoral efectors in earthworm innate immunity. In addition, our results possibly suggest that earthworm EaChi4 may function as a pattern recognition molecule modulating the downstream immune pathway.
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참고문헌 (26)
참고문헌 신청
Arakane Y / 2010 / Insect chitinase and chitinase-like proteins / Cell Mol Life Sci 67:201~216
Arakane Y / 2003 / Properties of catalytic, linker and chitin-binding domains of insect chitinase / Insect Biochem Mol Biol 33:631~648
Badariotti F / 2007 / Characterization of chitinase-like proteins(Cg-Clp1 and Cg-Clp2)involved in immune defence of the mollusc Crassostrea gigas / FEBS J 274:3646~3654
Badariotti F / 2007 / Characterization of an atypical family 18 chitinase from the oyster Crassostrea gigas : evidence for a role in early development and immunity / Dev Comp Immunol 31:559~570
Badariotti F / 2011 / Identifcation of three singular glycosyl hydrolase family 18 members from the oyster Crassostrea gigas : Structural characterization, phylogenetic analysis and gene expression / Comp Biochem Physiol B Biochem Mol Biol 158:56~63
Arakane Y / 2003 / Properties of catalytic, linker and chitin-binding domains of insect chitinase / Insect Biochem Mol Biol 33:631~648
Badariotti F / 2007 / Characterization of chitinase-like proteins(Cg-Clp1 and Cg-Clp2)involved in immune defence of the mollusc Crassostrea gigas / FEBS J 274:3646~3654
Badariotti F / 2007 / Characterization of an atypical family 18 chitinase from the oyster Crassostrea gigas : evidence for a role in early development and immunity / Dev Comp Immunol 31:559~570
Badariotti F / 2011 / Identifcation of three singular glycosyl hydrolase family 18 members from the oyster Crassostrea gigas : Structural characterization, phylogenetic analysis and gene expression / Comp Biochem Physiol B Biochem Mol Biol 158:56~63
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