Evidence indicating the existence of a novel family of serine protease inhibitors that may be involved in marine invertebrate immunity
A new serine protease inhibitor, designated cvSI-2, was purified and characterized from the plasma of the eastern oyster, Crassostrea virginica. CvSI-2 inhibited the serine protease subtilisin A in a slow-tight binding manner, with an overall dissociation constant Ki* of 0.18 nM. It also inhibited p...
Published in: | Fish & Shellfish Immunology |
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ftlouisianastuir:oai:digitalcommons.lsu.edu:animalsciences_pubs-1819 2023-06-11T04:15:49+02:00 Evidence indicating the existence of a novel family of serine protease inhibitors that may be involved in marine invertebrate immunity Xue, Qinggang Itoh, Naoki Schey, Kevin L. Cooper, Richard K. La Peyre, Jerome F. 2009-01-01T08:00:00Z https://digitalcommons.lsu.edu/animalsciences_pubs/820 https://doi.org/10.1016/j.fsi.2009.05.006 unknown LSU Digital Commons https://digitalcommons.lsu.edu/animalsciences_pubs/820 doi:10.1016/j.fsi.2009.05.006 Faculty Publications Bivalve mollusc Oyster Perkinsus marinus Protease inhibitor family Serine protease inhibitor Tunicate text 2009 ftlouisianastuir https://doi.org/10.1016/j.fsi.2009.05.006 2023-05-28T18:12:50Z A new serine protease inhibitor, designated cvSI-2, was purified and characterized from the plasma of the eastern oyster, Crassostrea virginica. CvSI-2 inhibited the serine protease subtilisin A in a slow-tight binding manner, with an overall dissociation constant Ki* of 0.18 nM. It also inhibited perkinsin, the major extracellular protease of the oyster protozoan parasite Perkinsus marinus. Sequencing of cvSI-2 cloned cDNA revealed an open reading frame of 258 bp encoding a polypeptide of 85 amino acids, with the 18 N-terminal amino acids forming a signal peptide. The mature cvSI-2 molecule predicted consisted of 67 amino acids with 12 cysteine residues and a calculated molecular mass of 7202.96 Da. Overall 91% of the cvSI-2 amino acid sequence predicted from cDNA was confirmed by tandem mass spectrometry sequencing of purified cvSI-2. In addition, serine 43 and a threonine substitution at this position were observed. CvSI-2 amino acid sequence showed a 38% identity and 54% similarity with that of cvSI-1, the first protease inhibitor purified and characterized from a bivalve mollusc. Like cvSI-1, cvSI-2 gene was expressed in the basophil cells of digestive tubules. BLAST search found multiple ESTs from the eastern oyster, Pacific oyster, Mediterranean mussel, and sea vase, a tunicate, which could encode proteins with sequences similar to cvSI-1 and cvSI-2. Our findings indicate that cvSI-1 and cvSI-2 are members of a novel family of serine protease inhibitors in bivalve molluscs and perhaps other marine invertebrates, which share the characteristic cysteine array C-X4-9-C-X4-6-C-X7-C-X4-C-T-C-X6-9-C-X5-C-X3-7-C-X6-10-C-X4-C-X-C. © 2009 Elsevier Ltd. All rights reserved. Text Pacific oyster LSU Digital Commons (Louisiana State University) Pacific Fish & Shellfish Immunology 27 2 250 259 |
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Open Polar |
collection |
LSU Digital Commons (Louisiana State University) |
op_collection_id |
ftlouisianastuir |
language |
unknown |
topic |
Bivalve mollusc Oyster Perkinsus marinus Protease inhibitor family Serine protease inhibitor Tunicate |
spellingShingle |
Bivalve mollusc Oyster Perkinsus marinus Protease inhibitor family Serine protease inhibitor Tunicate Xue, Qinggang Itoh, Naoki Schey, Kevin L. Cooper, Richard K. La Peyre, Jerome F. Evidence indicating the existence of a novel family of serine protease inhibitors that may be involved in marine invertebrate immunity |
topic_facet |
Bivalve mollusc Oyster Perkinsus marinus Protease inhibitor family Serine protease inhibitor Tunicate |
description |
A new serine protease inhibitor, designated cvSI-2, was purified and characterized from the plasma of the eastern oyster, Crassostrea virginica. CvSI-2 inhibited the serine protease subtilisin A in a slow-tight binding manner, with an overall dissociation constant Ki* of 0.18 nM. It also inhibited perkinsin, the major extracellular protease of the oyster protozoan parasite Perkinsus marinus. Sequencing of cvSI-2 cloned cDNA revealed an open reading frame of 258 bp encoding a polypeptide of 85 amino acids, with the 18 N-terminal amino acids forming a signal peptide. The mature cvSI-2 molecule predicted consisted of 67 amino acids with 12 cysteine residues and a calculated molecular mass of 7202.96 Da. Overall 91% of the cvSI-2 amino acid sequence predicted from cDNA was confirmed by tandem mass spectrometry sequencing of purified cvSI-2. In addition, serine 43 and a threonine substitution at this position were observed. CvSI-2 amino acid sequence showed a 38% identity and 54% similarity with that of cvSI-1, the first protease inhibitor purified and characterized from a bivalve mollusc. Like cvSI-1, cvSI-2 gene was expressed in the basophil cells of digestive tubules. BLAST search found multiple ESTs from the eastern oyster, Pacific oyster, Mediterranean mussel, and sea vase, a tunicate, which could encode proteins with sequences similar to cvSI-1 and cvSI-2. Our findings indicate that cvSI-1 and cvSI-2 are members of a novel family of serine protease inhibitors in bivalve molluscs and perhaps other marine invertebrates, which share the characteristic cysteine array C-X4-9-C-X4-6-C-X7-C-X4-C-T-C-X6-9-C-X5-C-X3-7-C-X6-10-C-X4-C-X-C. © 2009 Elsevier Ltd. All rights reserved. |
format |
Text |
author |
Xue, Qinggang Itoh, Naoki Schey, Kevin L. Cooper, Richard K. La Peyre, Jerome F. |
author_facet |
Xue, Qinggang Itoh, Naoki Schey, Kevin L. Cooper, Richard K. La Peyre, Jerome F. |
author_sort |
Xue, Qinggang |
title |
Evidence indicating the existence of a novel family of serine protease inhibitors that may be involved in marine invertebrate immunity |
title_short |
Evidence indicating the existence of a novel family of serine protease inhibitors that may be involved in marine invertebrate immunity |
title_full |
Evidence indicating the existence of a novel family of serine protease inhibitors that may be involved in marine invertebrate immunity |
title_fullStr |
Evidence indicating the existence of a novel family of serine protease inhibitors that may be involved in marine invertebrate immunity |
title_full_unstemmed |
Evidence indicating the existence of a novel family of serine protease inhibitors that may be involved in marine invertebrate immunity |
title_sort |
evidence indicating the existence of a novel family of serine protease inhibitors that may be involved in marine invertebrate immunity |
publisher |
LSU Digital Commons |
publishDate |
2009 |
url |
https://digitalcommons.lsu.edu/animalsciences_pubs/820 https://doi.org/10.1016/j.fsi.2009.05.006 |
geographic |
Pacific |
geographic_facet |
Pacific |
genre |
Pacific oyster |
genre_facet |
Pacific oyster |
op_source |
Faculty Publications |
op_relation |
https://digitalcommons.lsu.edu/animalsciences_pubs/820 doi:10.1016/j.fsi.2009.05.006 |
op_doi |
https://doi.org/10.1016/j.fsi.2009.05.006 |
container_title |
Fish & Shellfish Immunology |
container_volume |
27 |
container_issue |
2 |
container_start_page |
250 |
op_container_end_page |
259 |
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1768372946511855616 |