CSIR Central

Suppression of Macrophage Lysosomal Enzymes after Leishmania donovani Infection

IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata

View Archive Info
 
 
Field Value
 
Title Suppression of Macrophage Lysosomal Enzymes after Leishmania donovani Infection
 
Creator Chakraborty, Prasanta
Das, Pijush K
 
Subject Infectious Diseases and Immunology
 
Description Leishmania donovani is an obligate intracellular parasite residing in the pha-golysosome of the host’s mononuclear phagocytes (1). Infection with this parasite begins with the introduction by the sandfly vector of the flagellated promastigote into the blood stream, leading to intracellular parasitism of macrophages. Mac- rophages constitute one of the primary defense mechanisms of the body against microbial invasion and are capable of fulfilling a variety of microbicidal functions such as the production of free oxygen radicals and lysosomal enzymes and the ability to activate host’s immune system. The means used by Leishmania parasites to overcome the formidable array of macrophage’s killing response is one of the still unsolved mysteries of Leishmania biology. Work on other parasites which live in a similar environment has revealed several possible mechanisms. Thus Toxoplasma (2,3) and Tuber&e bacilli (4) appear to be able to prevent fusion of the destructive macrophage lysosomes with the phagocytic vacuole, whereas Mycobacterium lepraemurium achieves immunity through a physical barrier in the form of a thick enveloping capsule (5,6). Trypanosoma crud is able to escape from the original phagosome and live in direct contact with the cytoplasm (7), thus avoiding the essentially vacuole-bound lysosomal enzymes.
 
Date 1989
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/1387/1/BIOCHEMICAL_MEDICINE_AND_METABOLIC_BIOLOGY__Volume_41___Issue_1___Pages_46%2D55%2C1989[46].pdf
Chakraborty, Prasanta and Das, Pijush K (1989) Suppression of Macrophage Lysosomal Enzymes after Leishmania donovani Infection. Biochemical Medicine and Metabolic Biology, 41 (1). pp. 46-55.
 
Relation http://dx.doi.org/10.1016/0885-4505(89)90007-8
http://www.eprints.iicb.res.in/1387/