Matrix metalloproteinases activity demonstrated in the infective stage of the nematodes, Angiostrongylus cantonensis

Ingestion of the larval nematode Angiostrongylus cantonensis can cause the human eosinophilic meningitis known as angiostrongyliasis. Analysis of the extracts and excretory-secretory (ES) products of A. cantonensis larvae and adult stages on gelatin substrate zymography demonstrated the presence of distinct gelatinolytic enzymes. In worm extracts, inhibitor studies showed that the metalloproteinases revealed in L1 (23 kDa), L3 (66, 42 and 30 kDa), young adult worm (72 and 94 kDa) and adult worm (72 and 94 kDa). In ES products, the L1 revealed one low (42 kDa) and two high (105 and 94 kDa) molecular weight proteolytic bands that degraded gelatin in substrate gels. The L3 revealed three low (66, 50, and 30 kDa) and one high (105 kDa) molecular weight proteolytic bands. Inhibitor studies confirmed that the 105 and 94 proteolytic bands of the L1, and the 50 and 30 kDa proteolytic bands of the L3 classification were metalloproteinases. These metalloproteinases secreted in the infective larvae may be associated with the parasite dissemination or pathogenesis.