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Identification and characterization of two chitin-binding proteins from the peritrophic membrane of the silkworm,
Hua-Jun Yang1, Fang Zhou, Firdose Ahmad Malik
1Key Laboratory of Animal Epidemic Etiology & Immunological Prevention of Ministry of Agriculture, Zhejiang University, Hangzhou, People's Republic of China.
Abstract:
The peritrophic membrane (PM) is a semi-permeable lining of the insect midgut, broadly analogous to the mucous lining of vertebrate gut. The PM proteins are important achievements for the function of the PM. In this study, two chitin-binding proteins (BmPM-P43 and BmPM-P41) from the PM of the silkworm, Bombyx mori, were identified and cloned. These proteins showed the molecular mass of 43 and 41 kDa, respectively. The deduced amino acid sequences codes for a protein of 381 amino acid residues and 364 amino acid residues, containing 12 and 14 cysteine residues followed by similar domain, both of them have 5 cysteine residues in similar position in the C-terminal. The confirmation of these proteins was performed by western blot analysis of recombinant BmPM-P43 and BmPM-P41. The chitin-binding activity analysis showed that the BmPM-P43 and BmPM-P41 could bind to chitin strongly. It is concluded that BmPM-P43 and BmPM-P41 contains a polysaccharide deacetylase domain instead of peritrophin domain, indicated that these two proteins may belong to a new chitin-binding protein family.
Insights
Two novel chitin-binding proteins, BmPM-P43 and BmPM-P41, were identified in the silkworm peritrophic membrane (PM). These proteins exhibit strong chitin-binding activity and may represent a new family of chitin-binding proteins.
Area of Science:
- Insect molecular biology
- Biochemistry
- Protein science
Background:
- The peritrophic membrane (PM) is a crucial semi-permeable barrier in the insect midgut.
- PM proteins are essential for its structural integrity and function.
- Understanding these proteins aids in comprehending insect gut physiology.
Purpose of the Study:
- To identify and characterize novel chitin-binding proteins from the silkworm (Bombyx mori) peritrophic membrane.
- To investigate the functional properties of these identified proteins, specifically their chitin-binding capabilities.
- To determine the potential classification of these proteins within known protein families.
Main Methods:
- Identification and cloning of two candidate proteins, BmPM-P43 and BmPM-P41.
- Sequence analysis to determine protein size and identify conserved domains.
- Western blot analysis to confirm protein expression and identity.
- Chitin-binding activity assays to assess protein-chitin interaction.
Main Results:
- Two proteins, BmPM-P43 (43 kDa) and BmPM-P41 (41 kDa), were successfully identified and cloned.
- Amino acid sequence analysis revealed specific cysteine residue patterns and a conserved domain.
- Western blot confirmed the recombinant proteins.
- Both BmPM-P43 and BmPM-P41 demonstrated strong binding affinity to chitin.
- The proteins possess a polysaccharide deacetylase domain, not a peritrophin domain.
Conclusions:
- BmPM-P43 and BmPM-P41 are novel chitin-binding proteins from the Bombyx mori peritrophic membrane.
- These proteins exhibit significant chitin-binding activity.
- The presence of a polysaccharide deacetylase domain suggests these proteins may constitute a new family of chitin-binding proteins.
