In vitro cultivation of Angiostrongylus costaricensis eggs to first stage larvae in chemically defined medium

In vitro cultivation of Angiostrongylus costaricensis eggs to first stage larvae in chemically defined medium

Abstracts /Parasitology International International Journal for Parasitology, Volume 26 (3) (19961, Page 281-286 In vitro cultivation of Angiostron...

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Abstracts /Parasitology

International

International Journal for Parasitology, Volume 26 (3) (19961, Page 281-286

In vitro cultivation of Angiostrongylus costuricensis eggs to first stage larvae in chemically defined medium

H. Hata Department of Parasitology, Chiba University, School of Medicine, Inohana, Chiba City 260, Japan Angiostrongylus costaricensis eggs were successfully cultured to first stage larvae ina chemically defined medium. The most suitable medium for development was Ham’s F-12 among seven chemically defined media and 10 serum supplemented media examined. The addition of serum to Ham’s F-12 did not provide any further benefits for egg development. When tile eggs were cultured in this medium under 8% CO, in air, they developed and formed larvae inside tile eggs 5 days later. Thereafter, the eggs began to hatch to first stage larvae. Ten days after cultivation, 33% of the eggs had developed to first stage larvae. When these first stage larvae were infected to tile snail intermediate host, Biomphalaria glabrata, they developed to third stage larvae.

46 (1997) 79-85

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trivolvis or E. caproni on days 10, 16 and 20 p.i. after primary infections of E. tivoluis metacercariae. Five-day-old juveniles of E. triuoluis and E. caproni, which were recovered from C3H mice or hamsters, were also used for challenge infections on day 10 p.i. The metacercariae and juveniles, which were challenged homologously and heterologously on day 10 p.i., were almost expelled. The metacercariae of E. trivofvis, which were challenged homologously on day 16, were completely rejected, but only a few challenged metacercariae of E. caproni in heterologous infection were recovered. Considerable numbers of E. caproni were recovered when challenge infections with the metacercariae were done on day 20 p.i., while only a small number of E. trivoZvis was recovered. All controls without primary infections showed a recovery rate of over 50% of the worms. These results indicate that increased secretion of mucins by hyperplastic goblet cells associatedwith primary infections of E. trivolvis may be responsible for the expulsion of worms challenged homologously with E. trivolvis and heterologously with E. caproni from the mouse host. Molecular and Biochemical 76 (1) (19961, Page 11-21

Parasitology Volume

26 (3)

Molecular cloning and expression of the gene encoding a cysteine proteinase of Spirometra erinacei

Rapid expulsion of the intestinal trematodes Echinostoma trivolvis and E. caproni from C3H mice by trapping with increased goblet cell mucins

Department of Parasitology, Shinshu University, School of Medicine, Asahi 3-l-l Matsumoto City, Nagano 390, Japan

International Journal (19961, Page 319-324

for Parasitology

D. Wu Liu, H. Kato, T. Nakamura, K. Sugane

T. Fujino, B. Fried, H. Ichikawa, I.Tada Department of Parasitoloa, Faculty of Medicine, Kyushu University Fukuoka 812, Japan Echinostoma t&o&s (Cort, 1914) adults wererejected from C3H mice by 15 days post-exposure, corresponding to the increase in the number of goblet cells. Homologous and heterologous infections with the allopatric species E. caproni (Richard, 1964) were used to confirm the effect of increased secretion of goblet cell mucins in rejecting metacercariae of challenge infections of E.

A cDNA library constructed from plerocercoid of Spirometraerinacei (SEP) was immunoscreened using rabbit anti-plerocercoid proteinase polyclonal antibody. A l.O-kb cDNA clone encoding a cysteine proteinase composed of 336 amino acids was isolated. The amino acid sequence predicted from the cDNA showed significant homology with human and mouse cathepsin L. N-terminal amino acid sequence of the native cysteine proteinase extracted from SEP was the same as that of mature proteinase predicted from the cloned