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Zoology and wildlife conservation

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Abstracts » Zoology and wildlife conservation

Human parasite finds taxonomic home

Article Abstract:

A systematic molecular study of the small-subunit ribosomal RNA of Blastocystis hominis places the parasite in the stramenopiles class. B. hominis is an obligatory anaerobic protist present in the human intestine. While it lacks flagella and flagellar hairs unlike other members of stramenopiles, its life cycle has certain similarities with that of its sister taxon Proteromonas. Stramenopiles is a complex and heterogeneous group that contains unicellular and multicellular protists, and heterotrophic and photosynthetic organisms.

Author: Sogin, Mitchell L., Silberman, Jeffrey D., Leipe, Detlef D., Clark, C. Graham
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
Identification and classification, Protista, Protists

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Skirmishes on the border

Article Abstract:

Yersinia, a genus of gram-negative pathogenic bacteria, gain entry to human epithelial cells by interacting with a normally noninvasive bacterium, Escherichia coli (E. coli). The Yersinia species are able to link themselves to E. coli using a cell surface protein called invasin. Yersinia's ability to infect epithelial cells only after the invasin gene was cloned in E. coli demonstrated the relationship between Yersinia and E. coli. However, much remains to be learned about how parasites and host cells affect each other.

Author: Donelson, John E., Fulton, Alice B.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
Hyaluronic acid, Yersinia infections

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Crystal structures explain functional properties of two E. coli porins

Article Abstract:

The gram-negative bacterium Escherichia coli has two porins structured as aqueous channels to assist in spreading small hydrophilic molecules across outer membranes. The two porins, matrix porin and phosphorin, are membrane proteins that ward off potentially harmful agents. Both porins show trimers of identical subunits, with each subunit being composed of a 16-stranded anti-parallel beta-barrel with a pore. This structure accounts for the porins' molecular function and for how those functions are changed by mutation.

Author: Cowan, S.W., Schirmer, T., Rummel, G., Steiert, M., Ghosh, R., Pauptit, R.A., Jansonius, J.N., Rosenbusch, J.P.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
Membrane proteins

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Subjects list: Research, Medical parasitology, Parasitology, Physiological aspects, Escherichia coli
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