12 research outputs found
Use of SMS texts for facilitating access to online alcohol interventions: a feasibility study
A41 Use of SMS texts for facilitating access to online alcohol interventions: a feasibility study
In: Addiction Science & Clinical Practice 2017, 12(Suppl 1): A4
Secretory leukoprotease inhibitor: partnering alpha 1-proteinase inhibitor to combat pulmonary inflammation.
Fine needle aspiration cytology diagnosis of malignant lymphoma and reactive lymphoid hyperplasia
Impaired recruitment of the small GTPase rab7 correlates with the inhibition of phagosome maturation by Leishmania donovani promastigotes
Predicting and explaining plant invasions through analysis of source area floras: some critical considerations
Virulence Attenuation of a UDP-galactose/ N-acetylglucosamine β1,4 Galactosyltransferase Expressing Leishmania donovani Promastigote
Protozoan parasites of the genus Leishmania are
the causative agent of leishmaniasis, a disease whose
manifestations in humans range from mild cutaneous
lesions to fatal visceral infections. Human visceral leishmaniasis
is caused by Leishmania donovani. Long-term
culture in vitro leads to the attenuation of the parasite. This
loss of parasite virulence is associated with the expression
of a developmentally regulated UDP-Galactose/N-acetylglucosamine
β 1–4 galactosyltransferase and galactose
terminal glycoconjugates as determined by their agglutination
with the pea nut agglutinin (PNA). Thus, all promastigotes
passaged for more than 11 times were 100%
agglutinated with PNA, and represent a homogeneous
population of avirulent parasites. Identical concentrations
of PNA failed to agglutinate promastigotes passaged for ≤5
times. These PNA− promastigotes were virulent. Promastigotes
passaged from 5 to 10 times showed a mixed
population. The identity of populations defined by virulence
and PNA agglutination was confirmed by isolating
PNA+ avirulent and PNA− virulent clones from the 7th
passage promastigotes. Only the PNA+ clones triggered
macrophage microbicidal activity. The PNA+ clones lacked lipophosphoglycan. Intravenous administration of [14C]
galactose-labeled parasite in BALB/c mice resulted in rapid
clearance of the parasite from blood with a concomitant
accumulation in the liver. By enzymatic assay and RT-PCR
we have shown the association of a UDP-Galactose/Nacetylglucosamine
β1,4 galactosyltransferase with only the
attenuated clones. By immunofluorescence we demonstrated
that the enzyme is located in the Golgi apparatus. By
western blot analysis and SDS-PAGE of the affinitypurified
protein, we have been able to identify a 29 KDa
galactose terminal protein from the avirulent clones