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PDBsum entry 3q6t
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Protein binding
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PDB id
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3q6t
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References listed in PDB file
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Key reference
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Title
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Structure and function of a "yellow" protein from saliva of the sand fly lutzomyia longipalpis that confers protective immunity against leishmania major infection.
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Authors
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X.Xu,
F.Oliveira,
B.W.Chang,
N.Collin,
R.Gomes,
C.Teixeira,
D.Reynoso,
V.My pham,
D.E.Elnaiem,
S.Kamhawi,
J.M.Ribeiro,
J.G.Valenzuela,
J.F.Andersen.
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Ref.
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J Biol Chem, 2011,
286,
32383-32393.
[DOI no: ]
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PubMed id
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Abstract
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LJM11, an abundant salivary protein from the sand fly Lutzomyia longipalpis,
belongs to the insect "yellow" family of proteins. In this study, we
immunized mice with 17 plasmids encoding L. longiplapis salivary proteins and
demonstrated that LJM11 confers protective immunity against Leishmania major
infection. This protection correlates with a strong induction of a delayed type
hypersensitivity (DTH) response following exposure to L. longipalpis saliva.
Additionally, splenocytes of exposed mice produce IFN-γ upon stimulation with
LJM11, demonstrating the systemic induction of Th1 immunity by this protein. In
contrast to LJM11, LJM111, another yellow protein from L. longipalpis saliva,
does not produce a DTH response in these mice, suggesting that structural or
functional features specific to LJM11 are important for the induction of a
robust DTH response. To examine these features, we used calorimetric analysis to
probe a possible ligand binding function for the salivary yellow proteins.
LJM11, LJM111, and LJM17 all acted as high affinity binders of prohemostatic and
proinflammatory biogenic amines, particularly serotonin, catecholamines, and
histamine. We also determined the crystal structure of LJM11, revealing a
six-bladed β-propeller fold with a single ligand binding pocket located in the
central part of the propeller structure on one face of the molecule. A
hypothetical model of LJM11 suggests a positive electrostatic potential on the
face containing entry to the ligand binding pocket, whereas LJM111 is negative
to neutral over its entire surface. This may be the reason for differences in
antigenicity between the two proteins.
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