Pm. Hine et B. Wesney, INTERACTION OF PHAGOCYTOSED BONAMIA SP (HAPLOSPORIDIA) WITH HEMOCYTESOF OYSTERS TIOSTREA-CHILENSIS, Diseases of aquatic organisms, 20(3), 1994, pp. 219-229
The interaction between the haplosporidian pathogen Bonamia sp. and th
e haemocytes of oysters Tiostrea chilensis was studied ultrastructural
ly and using ultracytochemistry for the lysosomal hydrolases, beta-gly
cerophosphatase (beta-GPase), cytidine monophosphatase (CMPase), thiam
ine pyrophosphatase (TPPase), and beta-galactosidase. Although fine an
d coarse granulocytes, serous (brown) cells and hyalinocytes were pres
ent, agranular precursors of fine granulocytes (progranulocytes), degr
anulated coarse granulocytes, hyalinocytes and serous cells commonly p
hagocytosed Bonamia sp. A sequence of infection from initial occupatio
n of tight phagosomes to formation of an enlarged phagosome or parasit
ophorous vacuole (PV), which sometimes broke down, occurred in all inf
ected haemocytes. Enlargement of the phagosome membrane to eventually
form a PV coincided with formation of bilaminar vesicles in the lipoid
bodies of parasites and their release from an indented area of the pa
rasite surface. Too few infected granulocytes were observed to determi
ne whether phagosome modification blocked lysosome-phagosome fusion. V
esicular CMPase and TPPase were produced by agranular haemocytes conta
ining phagocytosed Bonamia sp. and passed into tight phagosomes. Despi
te some endocytosis of these enzymes by Bonamia sp., very few parasite
s appeared dense or moribund. From the orientation of lipoid bodies to
ward the phagosome lumen, and release of beta-GPase into the lumen fro
m the lipoid bodies, parasite hydrolytic enzymes in lipoid bodies may
function in parasite nutrition, by extracellular digestion of host hae
mocyte cytoplasm.