In situ localization of heat-shock and histone proteins in honey-bee (Apis mellifera l.) larvae infected with Paenibacillus larvae.
The immunohistochemical localization of the heat shock proteins (Hsp70 and Hsp90) and histone protein in healthy and Paenibacillus larvae infected honeybee (Apis mellifera L.) larvae has been studied. Hsp70 was found in the nuclei and the cytoplasm of infected midgut, salivary gland cells and haemocytes, but not in uninfected larvae. Hsp90 was localized in both infected and uninfected cells. Exposed histone proteins were localized in the nuclei of dying uninfected cells undergoing programmed cell death. The distribution of histone protein in uninfected cells of midgut, salivary gland, and other tissues was nuclear and indicative of normal programmed cell death at levels between 1 and 5%. After applying histone protein antibodies to P. larvae infected honeybee larvae, the DAB based reaction product was located in the nuclei or immediate surroundings of all larval cells. The Hsp70, Hsp90 and histone protein distribution patterns are discussed in relation to the morphological, cytochemical and immunocytochemical characteristics of programmed cell death and pathological necrosis. Results produced by methyl green-pyronin staining confirm an elevation of RNA levels in normal programmed cell death and a reduced staining for RNA in necrotic infected cells.
Gregorc
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Veterinary Faculty of the University of Ljubljana, Gerbiceva 60, Ljubljana, 1000, Slovenia.
Bowen
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ID
D000818:Animals; D016863:Bacillaceae Infections / Q000378:metabolism*; D001407:Bacillus / Q000302:isolation & purification; D001516:Bees / Q000378:metabolism* / Q000382:microbiology; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D007150:Immunohistochemistry
D018840:HSP70 Heat-Shock Proteins; D018841:HSP90 Heat-Shock Proteins; D006657:Histones