Morphologic and morphometric characteristics of ascaroid worm, Ophidascaris piscatori in Xenochrophis piscator snake in Sidoarjo, Indonesia.

AIM: The study was conducted to describe the morphology and morphometry of nematode worm in the stomach of Xenochrophis piscator snake macroscopically and microscopically using light and scanning electron microscopy (SEM). MATERIALS AND METHODS: The sample was 40 nematode worms that have been collected from 60 snakes which slaughtered at snake slaughterhouses in Sidoarjo, Indonesia. The worms (10 male and 10 female) were stained with carmine, and the others were sent to Indonesian Science Institute for ultrastructure observation by SEM. Some of the female worms were immersed in physiological NaCl and incubated to collect the worm eggs. RESULTS: Nematode worm in this study had three lips with almost the same size and it had papillae, so it was included in ascaridoid. The mouth of ascaridoids has three lips, the dorsal bearing two large outer papillae and the each lateroventral with one papilla. The body length and width of the male worm were 70-105 mm and 0.92-1.32, respectively, with head diameter of 0.22-0.28 mm. Dorsal and ventrolateral lips almost have the same size that was 0.10-0.12×0.11-0.13 mm. The length of interlabia was 0.06-0.08 mm, esophagus was 3.21-4 mm, tail was 0.17-0.23 mm, and spicule was 2.12-3.36 mm. The body length and width of the female worm were 85-130 mm and 1.28-1.71 mm, respectively. The head diameter was 0.29-0.38 mm. Dorsal and ventrolateral lips almost have the same size that was 0.13-0.16×0.15-0.19 mm. The interlabial length was 0.08-0.10 mm, esophagus was 3.04-4.67 mm, and tail was 0.22-0.31 mm. The distance of the vulva from the anterior edge was 56-88 mm with an average of 67.35 mm. The eggs have conspicuously pitted with length 0.08-0.09 mm and width 0.07-0.08 mm. CONCLUSION: Based on the characteristics of morphology and morphometry, the ascaroid worms found on X. piscator snake from Sidoarjo, Indonesia, were O. piscatori.

A novel immunochromatographic system for easy-to-use detection of group 1 avian influenza viruses with acquired human-type receptor binding specificity.

A switch of viral hemagglutinin receptor binding specificity from bird-type α2,3- to human-type α2,6-linked sialic acid is necessary for an avian influenza virus to become a pandemic virus. In this study, an easy-to-use strip test to detect receptor binding specificity of influenza virus was developed. A biotinylated anti-hemagglutinin antibody that bound a broad range of group 1 influenza A viruses and latex-conjugated α2,3 (blue) and α2,6 (red) sialylglycopolymers were used in an immunochromatographic strip test, with avidin and lectin immobilized on a nitrocellulose membrane at test and control lines, respectively. Accumulation of a sialylglycopolymer-virus-antibody complex at the test line was visualized by eye. The strip test could be completed in 30min and did not require special equipment or skills, thereby avoiding some disadvantages of current methods for analyzing receptor binding specificity of influenza virus. The strip test could detect the receptor binding specificity of a wide range of influenza viruses, as well as small increases in the binding affinity of variant H5N1 viruses to α2,6 sialylglycans at viral titers >128 hemagglutination units. The strip test results were in agreement with those of ELISA virus binding assays, with correlations >0.95. In conclusion, the immunochromatographic strip test developed in this study should be useful for monitoring potential changes in the receptor binding specificity of group 1 influenza A viruses in the field.

Protease-dependent hemagglutinin cleavage contributes to alteration in chicken hemagglutination by the H3N2 influenza A virus.

The human influenza A virus (H3N2) has been the predominant influenza strain since 1992, and one property of this virus is non-agglutination of chicken erythrocytes [Ch(-) virus]. The Ch(-) virus in our study was able to acquire chicken hemagglutination [Ch(+)] by trypsin passage but not by chymotrypsin passage. Moreover, the trypsin-passaged Ch(+) viruses reacquired the Ch(-) property after a further chymotrypsin passage. In particular, genetic analysis showed no evidence of mutations in the hemagglutinin (HA) gene during either trypsin or chymotrypsin passages: the only differences found were in the HA cleavage sites between the trypsin-passaged virus and the chymotrypsin-passaged virus as determined by the N-terminal amino acid sequence. These results suggested that protease-dependent differences at the viral HA cleavage site, rather than genetic mutations, are likely to have a significant effect on the viral ability to produce chicken hemagglutination.

An H5N1 highly pathogenic avian influenza virus isolated from a local tree sparrow in Indonesia.

The isolation of an H5N1 influenza A virus from a tree sparrow (Passer montanus) captured in East Java, Indonesia in 2010 is reported here. Its hemagglutinin and neuraminidase were genetically similar to those of human isolates from 2006-2007 in Indonesia. The finding of a tree sparrow H5N1 virus that possesses genetically similar surface molecules to those of human viruses highlights the importance of monitoring resident wild birds, as well as migratory birds, for pandemic preparedness.