title: Angiostrongylus cantonensis cathepsin B-like protease (Ac-cathB-1) is involved in host gut penetration.
abstract: 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.
authors.affiliation: School of Life Sciences, Xiamen University, Fujian 361102, P.R. China - State Key Laboratory of Cellular Stress Biology, Xiamen University, Fujian 361102, P.R. China.
authors.forename: Ying
authors.initials: Y
authors.lastname: Long
authors.affiliation: School of Life Sciences, Xiamen University, Fujian 361102, P.R. China - State Key Laboratory of Cellular Stress Biology, Xiamen University, Fujian 361102, P.R. China.
authors.forename: Binbin
authors.initials: B
authors.lastname: Cao
authors.affiliation: School of Life Sciences, Xiamen University, Fujian 361102, P.R. China - State Key Laboratory of Cellular Stress Biology, Xiamen University, Fujian 361102, P.R. China.
authors.forename: Liang
authors.initials: L
authors.lastname: Yu
authors.affiliation: School of Life Sciences, Xiamen University, Fujian 361102, P.R. China - State Key Laboratory of Cellular Stress Biology, Xiamen University, Fujian 361102, P.R. China.
authors.forename: Meks
authors.initials: M
authors.lastname: Tukayo
authors.affiliation: School of Life Sciences, Xiamen University, Fujian 361102, P.R. China - State Key Laboratory of Cellular Stress Biology, Xiamen University, Fujian 361102, P.R. China.
authors.forename: Chonglv
authors.initials: C
authors.lastname: Feng
authors.affiliation: Medical College, Xiamen University, Fujian 361102, P.R. China.
authors.forename: Yinan
authors.initials: Y
authors.lastname: Wang
authors.affiliation: School of Life Sciences, Xiamen University, Fujian 361102, P.R. China - State Key Laboratory of Cellular Stress Biology, Xiamen University, Fujian 361102, P.R. China.
authors.forename: Damin
authors.initials: D
authors.lastname: Luo
mesh_terms: D017185:Angiostrongylus cantonensis / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development / Q000502:physiology; D000818:Animals; D002401:Cathepsin B / Q000037:antagonists & inhibitors / Q000235:genetics / Q000276:immunology / Q000302:isolation & purification / Q000502:physiology*; D002460:Cell Line; D004789:Enzyme Activation; D004847:Epithelial Cells / Q000469:parasitology; D016326:Extracellular Matrix Proteins / Q000378:metabolism; D005822:Genetic Vectors / Q000235:genetics; D015801:Helminth Proteins / Q000037:antagonists & inhibitors / Q000235:genetics / Q000276:immunology / Q000302:isolation & purification / Q000502:physiology*; D006790:Host-Parasite Interactions; D006868:Hydrolysis; D007106:Immune Sera; D007411:Intestinal Diseases, Parasitic / Q000201:enzymology* / Q000469:parasitology; D007422:Intestines / Q000469:parasitology; D007814:Larva; D016086:Lentivirus / Q000235:genetics; D051379:Mice; D051381:Rats; D017207:Rats, Sprague-Dawley; D011993:Recombinant Fusion Proteins / Q000302:isolation & purification / Q000378:metabolism; D012908:Snails / Q000469:parasitology; D017206:Strongylida Infections / Q000201:enzymology* / Q000469:parasitology
chemical_list: D016326:Extracellular Matrix Proteins; D015801:Helminth Proteins; D007106:Immune Sera; D011993:Recombinant Fusion Proteins; D002401:Cathepsin B