Angiostrongylus cantonensis cathepsin B-like protease (Ac-cathB-1) is involved in host gut penetration
Although the global spread of the emerging zoonosis, human angiostrongyliasis, has attracted increasing attention, understanding of specific gene function has been impeded by the inaccessibility of genetic manipulation of the pathogen nematode causing this disease, Angiostrongylus cantonensis. Many...
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| Format: | Article |
| Language: | English |
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EDP Sciences
2015-01-01
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| Series: | Parasite |
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| Online Access: | http://dx.doi.org/10.1051/parasite/2015037 |
| _version_ | 1797641252937662464 |
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| author | Long Ying Cao Binbin Yu Liang Tukayo Meks Feng Chonglv Wang Yinan Luo Damin |
| author_facet | Long Ying Cao Binbin Yu Liang Tukayo Meks Feng Chonglv Wang Yinan Luo Damin |
| author_sort | Long Ying |
| collection | DOAJ |
| description | Although the global spread of the emerging zoonosis, human angiostrongyliasis, has attracted increasing attention, understanding of specific gene function has been impeded by the inaccessibility of genetic manipulation of the pathogen nematode causing this disease, Angiostrongylus cantonensis. Many parasitic proteases play key roles in host-parasite interactions, but those of A. cantonensis are always expressed as the inactive form in prokaryotic expression systems, thereby impeding functional studies. Hence, a lentiviral system that drives secreted expression of target genes fused to a Myc-His tag was used to obtain recombinant Ac-cathB-1 with biological activity. Although this class of proteases was always reported to function in nutrition and immune evasion in parasitic nematodes, recombinant Ac-cathB-1 was capable of hydrolysis of fibronectin and laminin as well as the extracellular matrix of IEC-6 monolayer, so that the intercellular space of the IEC-6 monolayer increased 5.15 times as compared to the control, while the shape of the adherent cells partly rounded up. This suggests a probable role for this protease in intestinal epithelial penetration. The inhibition of Ac-cathB-1 enzymatic activity with antiserum partly suppressed larval penetration ability in the isolated intestine. Thus, an effective system for heterologous expression of parasite proteases is presented for studying gene function in A. cantonensis; and Ac-cathB-1 was related to larval penetration ability in the host small intestine. |
| first_indexed | 2024-03-11T13:42:27Z |
| format | Article |
| id | doaj.art-956ea2b546914f6d850f832b02ec6eaf |
| institution | Directory Open Access Journal |
| issn | 1776-1042 |
| language | English |
| last_indexed | 2024-03-11T13:42:27Z |
| publishDate | 2015-01-01 |
| publisher | EDP Sciences |
| record_format | Article |
| series | Parasite |
| spelling | doaj.art-956ea2b546914f6d850f832b02ec6eaf2023-11-02T11:20:17ZengEDP SciencesParasite1776-10422015-01-01223710.1051/parasite/2015037parasite150074Angiostrongylus cantonensis cathepsin B-like protease (Ac-cathB-1) is involved in host gut penetrationLong YingCao BinbinYu LiangTukayo MeksFeng ChonglvWang YinanLuo DaminAlthough the global spread of the emerging zoonosis, human angiostrongyliasis, has attracted increasing attention, understanding of specific gene function has been impeded by the inaccessibility of genetic manipulation of the pathogen nematode causing this disease, Angiostrongylus cantonensis. Many parasitic proteases play key roles in host-parasite interactions, but those of A. cantonensis are always expressed as the inactive form in prokaryotic expression systems, thereby impeding functional studies. Hence, a lentiviral system that drives secreted expression of target genes fused to a Myc-His tag was used to obtain recombinant Ac-cathB-1 with biological activity. Although this class of proteases was always reported to function in nutrition and immune evasion in parasitic nematodes, recombinant Ac-cathB-1 was capable of hydrolysis of fibronectin and laminin as well as the extracellular matrix of IEC-6 monolayer, so that the intercellular space of the IEC-6 monolayer increased 5.15 times as compared to the control, while the shape of the adherent cells partly rounded up. This suggests a probable role for this protease in intestinal epithelial penetration. The inhibition of Ac-cathB-1 enzymatic activity with antiserum partly suppressed larval penetration ability in the isolated intestine. Thus, an effective system for heterologous expression of parasite proteases is presented for studying gene function in A. cantonensis; and Ac-cathB-1 was related to larval penetration ability in the host small intestine.http://dx.doi.org/10.1051/parasite/2015037Lentiviral expressionAngiostrongylus cantonensisRecombinant Ac-cathB-1Protease |
| spellingShingle | Long Ying Cao Binbin Yu Liang Tukayo Meks Feng Chonglv Wang Yinan Luo Damin Angiostrongylus cantonensis cathepsin B-like protease (Ac-cathB-1) is involved in host gut penetration Parasite Lentiviral expression Angiostrongylus cantonensis Recombinant Ac-cathB-1 Protease |
| title | Angiostrongylus cantonensis cathepsin B-like protease (Ac-cathB-1) is involved in host gut penetration |
| title_full | Angiostrongylus cantonensis cathepsin B-like protease (Ac-cathB-1) is involved in host gut penetration |
| title_fullStr | Angiostrongylus cantonensis cathepsin B-like protease (Ac-cathB-1) is involved in host gut penetration |
| title_full_unstemmed | Angiostrongylus cantonensis cathepsin B-like protease (Ac-cathB-1) is involved in host gut penetration |
| title_short | Angiostrongylus cantonensis cathepsin B-like protease (Ac-cathB-1) is involved in host gut penetration |
| title_sort | angiostrongylus cantonensis cathepsin b like protease ac cathb 1 is involved in host gut penetration |
| topic | Lentiviral expression Angiostrongylus cantonensis Recombinant Ac-cathB-1 Protease |
| url | http://dx.doi.org/10.1051/parasite/2015037 |
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