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Characterization of kenyan isolates of Leishmania by Cellulose acetate electrophoresis

Published online by Cambridge University Press:  19 September 2011

N. N. Massamba ,
M. J. Mutinga  and
B. N. Odero
N. N. Massamba
Affiliation:
The International Centre of Insect Physiology and Ecology (ICIPE), P.O. Box 30772, Nairobi, Kenya
M. J. Mutinga
Affiliation:
The International Centre of Insect Physiology and Ecology (ICIPE), P.O. Box 30772, Nairobi, Kenya
B. N. Odero
Affiliation:
The International Centre of Insect Physiology and Ecology (ICIPE), P.O. Box 30772, Nairobi, Kenya
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Abstract

Thirty-eight Leishmania isolates from different host species (humans, mammals, reptiles and sandflies) from various parts of Kenya were compared with six World Health Organization Leishmania reference strains. Isoenzyme variations were assessed on the basis of their electrophoretic profiles on cellulose acetate membranes. Out of 18 enzymes studied, Five were selected for differentiating the Leishmania isolates. These were glucose-6-phosphate dehydrogenase (G6PD, E. C. 1. 1. 1. 49), glucose phosphate isomerase (GPI, E. C. 5. 3. 1. 9), malate dehydrogenase (MDH, E. C. 1. 1. 1. 37), mannose phosphate isomerase (MPI, E. C. 5. 3. 1. 8) and phosphoglucomutase (PGM, E. C. 2. 7. 5. 1).

Twenty-one isolates showed enzymatic patterns identical to the Leishmania reference strain Leishmania major IC-236, five isolates were similar to the Leishmania reference strain L. donovani IC-245 and three isolates were identical to the Leishmania reference strain L. aethiopica IC-228.

However, nine Leishmania isolates could not be identified by this method. They are either leishmanial species for which more Leishmania reference strains are needed for comparison or unidentified flagellates species.

The banding patterns revealed by L. major IC-235, isolated from Israel, were different from those of L. major IC-236, isolated from Kenya, with respect to G6PD; GPI; MDH; MPI and PGM.

Résumé

Trente-huit nouveaux isolats de Leishmania de différentes origines humaine et animale (hommes, chats sauvages, chèvres, lézards et phlébotomes) obtenus à travers le Kenya sont comparés avec des souches de référence de l'Organisation Mondiale de la Santé.

Les variations isoenzymatiques ont été déterminées en se basant sur leurs profits électrophorétiques sur membrane d'acétate de cellulose. Des dix-huit enzymes analysés, cinq ont été séléctionnés pour différencier les isolats de Leishmania. II s'agit du glucose-6-phosphate déshydrogenase (G6PD, E. C. 1. 1. 1. 49), glucose phosphate isomerase (GPI, E. C. 5. 3. 1. 9), malate déshydrogenase (MDH, E. C. 1. 1. 1. 37), mannose phosphate isomerase (MPI, E. C. 5. 3. 1. 8) et phosphoglucomutase (PGM, E. C. 2. 7. 5. 1).

Vingt et un isolats ont montré des profils enzymatiques identiques à ceux de la souche de référence Leishmania major IC-236, cinq étaient similaires à la souche de référence L. donovani IC 245 et trois isolats étaient identiques à la souche de référence L. aethiopica IC-228.

Cependant neuf isolats n'ont pas pu être identifiés par la méthode utilisée. IIs sont probablement identiques aux espèces déjà connues pour lesquelles des souches de référence sont nécessaires pour la comparaison ou d'autres espèces flagellées non identifiées de la famille de Kinoplastidae.

Les données présentées dans cet article indiquent aussi que les profils électrophorétiques obtenus avec la souche de référence L. major IC-235 en provenance d'Israel étaient très différents de ceux obtenus avec la souche de référence L. major IC-236 originaire du Kenya par rapport aux enzymes G6PD; GPI; MDH; MPI et PGM. Les implications épidémiologiques de ces données ont été discutées.

Keywords

Leishmania isolatesreference strainsenzyme typingLeishmania majorLeishmania aethiopicaLeishmania donovaniLeishmaniasouche de référencetypage enzymatiqueLeishmania majorLeishmania aethiopicaLeishmania donovani
Type
Research Articles
Information
International Journal of Tropical Insect Science , Volume 14 , Issue 2 , April 1993 , pp. 153 - 161
Copyright
Copyright © ICIPE 1993

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