Mycoplasma Gallisepticum Overview in Poultry
نویسندگان
چکیده
منابع مشابه
Detection of Mycoplasma gallisepticum and Mycoplasma synoviae among Commercial Poultry in Khouzestan Province, Iran
Mycoplasmas are important avian pathogens, which can cause both respiratory disease and synovitis in poultry that result in considerable economic losses to the poultry industry all over the world. The aim of this study was to determine the prevalence of Mycoplasma gallisepticum and Mycoplasma synoviae infections among commercial poultry flocks in ...
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Chronic Respiratory Disease (CRD) is caused by Mycoplasmas gallisepticum (MG) and is prevailing in layer, broiler and breeder poultry flocks. The infected birds showed sneezing, rales, coughing and exudates from nostrils and eyes. Mycoplasma species were recovered 27.3% overall, 39.3 per cent of the tracheal swabs, 15.9 per cent of tracheal tissues, 27.4 per cent of lung tissues and 25 per cent...
متن کاملMolecular characterization of Mycoplasma gallisepticum strains from South African poultry
This dissertation is dedicated to my parents Mamatsaba and Ohentse, my siblings Lerato and Lebogang, my cousin siblings Diau, Keneilwe, Ntsane and my grandmother Sponkie. 2 Acknowledgements I would like to express my deepest gratitude to the following: God, for I am a product of his mercy and love. This has been a successful year and I know I could not have done it alone. Thank you Father. Prof...
متن کاملAvian mycoplasmosis (Mycoplasma gallisepticum).
Mycoplasma gallisepticum is the most economically significant mycoplasma pathogen of poultry, and has a world-wide distribution. In common with other mycoplasmas, M. gallisepticum is minute in size with minimal genetic information and with a total lack of a bacterial cell wall. These properties are reflected in a high degree of interdependence between M. gallisepticum and the host animal, and i...
متن کاملNeuraminidase activity in Mycoplasma gallisepticum.
The whole viable Mycoplasma gallisepticum (strain TT) organisms were found to possess neuraminidase activity with a pH optimum of 5.8 on substrates such as human transferrin, human alpha(1)-glycoprotein, and rabbit serum. The enzyme operated optimally at pH 4.5 when N-acetylneuraminyl-lactose was used as the test substrate.
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ژورنال
عنوان ژورنال: American Journal of Biomedical Science & Research
سال: 2019
ISSN: 2642-1747
DOI: 10.34297/ajbsr.2019.04.000833