Literature summary for 3.6.1.5 extracted from

Maia, A.C.R.G.; Porcino, G.N.; Faria-Pinto, P.; Mendes, T.V.; Antinarelli, L.M.R.; Coimbra, E.S.; Reis, A.B.; Juliano, L.; Juliano, M.A.; Marques, M.J.; Vasconcelos, E.G.
Leishmania infantum nucleoside triphosphate diphosphohydrolase 1 (NTPDase 1) B-domain Antibody antiproliferative effect on the promastigotes and IgG subclass responses in canine visceral leishmaniasis (2019), Vet. Parasitol., 271, 38-44 .

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Application

Application	Comment	Organism
analysis	immune sera that recognize specifically the B domain of NTPDase 1 are produced against synthetic peptides (LbB1LJ and LbB2LJ) derived from this domain of NTPDase from Leishmania brasiliensis. The polyclonal antibodies have effective anti-leishmanial effect, reducing significantly in vitro promastigotes growth (21-25%), an antiproliferative effect is also demonstrated by immune sera produced against recombinant r-pot B domain, and two other synthetic peptides (potB1LJ and potB2LJ). In addition, using these biomolecules in ELISA technique, IgG1 and IgG2 subclasses reactivities of either healthy dogs or infected by Leishmania infantum and classified clinically as asymptomatic, oligosymptomatic and symptomatic are tested. Analysis of distinct IgG1 and IgG2 seropositivities patterns suggest antibody subclasses binding epitopes along B domain for protection against infection, indicating this domain as a tool for prophylactic and immunotherapeutic investigations	Leishmania infantum
analysis	immune sera that recognize specifically the B domain of NTPDase 1 are produced against synthetic peptides (LbB1LJ and LbB2LJ) derived from this domain of NTPDase from Leishmania brasiliensis. The polyclonal antibodies have effective anti-leishmanial effect, reducing significantly in vitro promastigotes growth (21-25%), an antiproliferative effect is also demonstrated by immune sera produced against recombinant r-pot B domain, and two other synthetic peptides (potB1LJ and potB2LJ). In addition, using these biomolecules in ELISA technique, IgG1 and IgG2 subclasses reactivities of either healthy dogs or infected by Leishmania infantum and classified clinically as asymptomatic, oligosymptomatic and symptomatic are tested. Analysis of distinct IgG1 and IgG2 seropositivities patterns suggest antibody subclasses binding epitopes along B domain for protection against infection, indicating this domain as a tool for prophylactic and immunotherapeutic investigations	Leishmania braziliensis

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cell surface	-	Leishmania infantum	9986	-
cell surface	-	Leishmania braziliensis	9986	-
flagellum	-	Leishmania infantum	-	-
flagellum	-	Leishmania braziliensis	-	-
kinetoplast	-	Leishmania infantum	20023	-
kinetoplast	-	Leishmania braziliensis	20023	-

Organism

Organism	UniProt	Comment	Textmining
Leishmania braziliensis	A4H7X3	-	-
Leishmania infantum	A4HWA0	-	-
Leishmania infantum MHOM/BR/1972/BH46	A4HWA0	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
promastigote	-	Leishmania infantum	-
promastigote	-	Leishmania braziliensis	-

Synonyms

Synonyms	Comment	Organism
LBRM_15_0030	-	Leishmania braziliensis
LINJ_15_0030	-	Leishmania infantum
NTPDase 1	-	Leishmania infantum
NTPDase 1	-	Leishmania braziliensis
nucleoside triphosphate diphosphohydrolase 1	-	Leishmania infantum
nucleoside triphosphate diphosphohydrolase 1	-	Leishmania braziliensis

General Information

General Information	Comment	Organism
additional information	immune sera that recognize specifically the B domain of NTPDase 1 are produced against synthetic peptides (LbB1LJ (residues 82-103, RERFKRIEPGLSSFATDQEGAK) and LbB2LJ (residues 102-121, AKQSLAGLLRFAEKAVPRSY) synthetic peptides belong to the N- and C-terminal portions, respectively) derived from this domain. The polyclonal antibodies have effective anti-leishmanial effect, reducing significantly in vitro promastigotes growth (21-25%), an antiproliferative effect is also demonstrated by immune sera produced against recombinant r-pot B domain, and two other synthetic peptides (potB1LJ and potB2LJ). In addition, using these biomolecules in ELISA technique, IgG1 and IgG2 subclasses reactivities of either healthy dogs or infected by Leishmania infantum and classified clinically as asymptomatic, oligosymptomatic and symptomatic are tested. The peptides have have high identity with their Leishmnia infantum NTPDase 1 counterparts. Analysis of distinct IgG1 and IgG2 seropositivities patterns suggest antibody subclasses binding epitopes along B domain for protection against infection, indicating this domain as a tool for prophylactic and immunotherapeutic investigations	Leishmania braziliensis
additional information	immune sera that recognize specifically the B domain of NTPDase 1 are produced against synthetic peptides (LbB1LJ and LbB2LJ) derived from this domain. The polyclonal antibodies have effective anti-leishmanial effect, reducing significantly in vitro promastigotes growth (21-25%), an antiproliferative effect is also demonstrated by immune sera produced against recombinant r-pot B domain, and two other synthetic peptides (potB1LJ and potB2LJ). The LbB1LJ (residues 82-103, RERFKRIEPGLSSFATDQEGAK) and LbB2LJ (residues 102-121, AKQSLAGLLRFAEKAVPRSY) synthetic peptides belong to the N- and C-terminal portions, respectively, from conserved B domain (82-121) of Leishmania braziliensis NTPDase 1 (UniProt ID A4H7X3), and have high identity with their Leishmnia infantum NTPDase 1 counterparts. In addition, using these biomolecules in ELISA technique, IgG1 and IgG2 subclasses reactivities of either healthy dogs or infected by Leishmania infantum and classified clinically as asymptomatic, oligosymptomatic and symptomatic are tested. Analysis of distinct IgG1 and IgG2 seropositivities patterns suggest antibody subclasses binding epitopes along B domain for protection against infection, indicating this domain as a tool for prophylactic and immunotherapeutic investigations	Leishmania infantum

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Release 2023.1 (January 2023)