2jo7: Difference between revisions

Line 4:

==Overview==

Babesia divergens is the Apicomplexa agent of the bovine babesiosis in, Europe: this infection leads to growth and lactation decrease, so that, economical losses due to this parasite are sufficient to require the, development of a vaccine. The major surface antigen of B. divergens has, been described as a 37 kDa protein glycosyl phosphatidyl inositol, (GPI)-anchored at the surface of the merozoite. The immuno-prophylactic, potential of Bd37 has been demonstrated, and we present here the, high-resolution solution structure of the 27 kDa structured core of Bd37, (Delta-Bd37) using NMR spectroscopy. A model for the whole protein has, been obtained using additional small angle X-ray scattering (SAXS) data., The knowledge of the 3D structure of Bd37 allowed the precise epitope, mapping of antibodies on its surface. Interestingly, the geometry of, Delta-Bd37 reveals an intriguing similarity with the exocyst subunit, Exo84p C-terminal region, an eukaryotic protein that has a direct, implication in vesicle trafficking. This strongly suggests that, Apicomplexa have developed in parallel molecular machines similar in, structure and function to the ones used for endo- and exocytosis in, eukaryotic cells.

Babesia divergens is the Apicomplexa agent of the bovine babesiosis in Europe: this infection leads to growth and lactation decrease, so that economical losses due to this parasite are sufficient to require the development of a vaccine. The major surface antigen of B. divergens has been described as a 37 kDa protein glycosyl phosphatidyl inositol (GPI)-anchored at the surface of the merozoite. The immuno-prophylactic potential of Bd37 has been demonstrated, and we present here the high-resolution solution structure of the 27 kDa structured core of Bd37 (Delta-Bd37) using NMR spectroscopy. A model for the whole protein has been obtained using additional small angle X-ray scattering (SAXS) data. The knowledge of the 3D structure of Bd37 allowed the precise epitope mapping of antibodies on its surface. Interestingly, the geometry of Delta-Bd37 reveals an intriguing similarity with the exocyst subunit Exo84p C-terminal region, an eukaryotic protein that has a direct implication in vesicle trafficking. This strongly suggests that Apicomplexa have developed in parallel molecular machines similar in structure and function to the ones used for endo- and exocytosis in eukaryotic cells.

==About this Structure==

Line 28:

[[Category: surface antigen]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Jan 23 11~~:42:29 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:04:32 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==Overview==
-Babesia divergens is the Apicomplexa agent of the bovine babesiosis in, Europe: this infection leads to growth and lactation decrease, so that, economical losses due to this parasite are sufficient to require the, development of a vaccine. The major surface antigen of B. divergens has, been described as a 37 kDa protein glycosyl phosphatidyl inositol, (GPI)-anchored at the surface of the merozoite. The immuno-prophylactic, potential of Bd37 has been demonstrated, and we present here the, high-resolution solution structure of the 27 kDa structured core of Bd37, (Delta-Bd37) using NMR spectroscopy. A model for the whole protein has, been obtained using additional small angle X-ray scattering (SAXS) data., The knowledge of the 3D structure of Bd37 allowed the precise epitope, mapping of antibodies on its surface. Interestingly, the geometry of, Delta-Bd37 reveals an intriguing similarity with the exocyst subunit, Exo84p C-terminal region, an eukaryotic protein that has a direct, implication in vesicle trafficking. This strongly suggests that, Apicomplexa have developed in parallel molecular machines similar in, structure and function to the ones used for endo- and exocytosis in, eukaryotic cells.
+Babesia divergens is the Apicomplexa agent of the bovine babesiosis in Europe: this infection leads to growth and lactation decrease, so that economical losses due to this parasite are sufficient to require the development of a vaccine. The major surface antigen of B. divergens has been described as a 37 kDa protein glycosyl phosphatidyl inositol (GPI)-anchored at the surface of the merozoite. The immuno-prophylactic potential of Bd37 has been demonstrated, and we present here the high-resolution solution structure of the 27 kDa structured core of Bd37 (Delta-Bd37) using NMR spectroscopy. A model for the whole protein has been obtained using additional small angle X-ray scattering (SAXS) data. The knowledge of the 3D structure of Bd37 allowed the precise epitope mapping of antibodies on its surface. Interestingly, the geometry of Delta-Bd37 reveals an intriguing similarity with the exocyst subunit Exo84p C-terminal region, an eukaryotic protein that has a direct implication in vesicle trafficking. This strongly suggests that Apicomplexa have developed in parallel molecular machines similar in structure and function to the ones used for endo- and exocytosis in eukaryotic cells.
 ==About this Structure==
@@ Line 28: / Line 28: @@
 [[Category: surface antigen]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:42:29 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:04:32 2008''