Immunogenic and antigenic properties of recombinant soluble glycoprotein of rabies virus

2005 ◽  
Vol 108 (3-4) ◽  
pp. 207-214 ◽  
Author(s):  
Praveen K. Gupta ◽  
Sameer Sharma ◽  
Sameer S. Walunj ◽  
V.K. Chaturvedi ◽  
Ashwin A. Raut ◽  
...  
Vaccine ◽  
1999 ◽  
Vol 17 (3) ◽  
pp. 205-218 ◽  
Author(s):  
Shin-ichi Sakamoto ◽  
Toshio Ide ◽  
Sachio Tokiyoshi ◽  
Junji Nakao ◽  
Fukusaburo Hamada ◽  
...  

1932 ◽  
Vol 50 (4) ◽  
pp. 367-376 ◽  
Author(s):  
L. C. Havens ◽  
C. R. Mayfield

1966 ◽  
Vol 16 (03/04) ◽  
pp. 559-573 ◽  
Author(s):  
L Uszyński

SummaryRabbits immunized against human AHG fibrinogen-free preparations, were shown to produce anti-AHG antibodies. The inhibitory activity of these antibodies was tested by thromboplastin generation test, thrombelastography, and the specific anti-AHG antibodies neutralization test. The latter test permitted quantitative determination of antigenic form of factor VIII. The inhibitory activity of anti-FI-O-Ta serum resulted exclusively from the anti-AHG antibodies which in coagulation tests behaved like circulating anticoagulants directed against factor VIII.The anti-AHG antibodies were neutralizable by normal human serum or plasma even contained only trace of AHG activity after storage. There was no antigenic form of factor VIII in the severely affected patients with hemophilia A, von Willebrand’s disease nor in the normal plasma adsorbed on bentonite. The presented results suggest a molecular defect of factor VIII in patients with hemophilia A. The severe form of this disease depends, probably, on a major impairment of AHG biosynthesis, leading to changes in the antigenic properties of the molecule. The AHG from rabbit, porcine and bovine plasma respectively did not neutralize the anti-AHG antibodies formed in rabbits immunized against human factor VIII preparations.


1969 ◽  
Vol 62 (1_Suppl) ◽  
pp. S13-S30 ◽  
Author(s):  
W. R. Butt

ABSTRACT Several chemical differences between FSH, LH and HCG have been reported: thus LH and HCG are richer in proline than FSH and FSH and HCG contain more N-acetyl neuraminic acid than LH. Sub-units of LH are formed by treatment with urea, guanidine or acid. HCG also may contain two sub-units. The sub-units from LH are biologically inert but retain their immunological activity: biological activity is restored when the sub-units are incubated together. There is much evidence from chemical and enzymic reactions that antigenic groups are distinct from those parts of the molecule essential for biological activity. N-acetyl neuraminic acid and probably other carbohydrates in FSH and HCG are not involved in immunological activity but are necessary for biological activity. Histidine, methionine and possibly cysteine appear to be essential for biological but not immunological activity of FSH, while tryptophan and possibly tyrosine are not essential for either. A few highly specific antisera to gonadotrophins have been prepared in rabbits and guinea pigs to crude antigens: there is no evidence that purified antigens are more likely to produce specific antisera. Differences in the immunological reactivities of urinary compared with pituitary gonadotrophins have been observed both by radioimmunoassay and by the complement fixation technique. The latter may be particularly useful for detecting structural differences in the hormones.


Author(s):  
Shay-Anne Daniels ◽  
Elizabeth M King ◽  
Christopher J Olivier ◽  
John PD Harding ◽  
Christine Fehlner-Gardiner ◽  
...  

Author(s):  
A. G. Mukhamedzhanova ◽  
◽  
M. A. Efimova ◽  
A. N. Chernov ◽  
K. S. Khaertynov ◽  
...  

Author(s):  
V. A. Babak ◽  
A. A. Gusev ◽  
I. A. Puntus ◽  
A. S. Smailova

The results of alternative studies on the immunogenic activity of live rabies vaccines for oral immunization of wild carnivorous animals are presented. The method of evaluation of immunogenicity using a model of oral immunization in mice with experimental infection control rabies virus CVS in the dose of 10–100 MLD50/0,03 ml. Once entered immunizing dose for white mice, weighing 12–14 g were 56.200 MLD50, the titers of VNA ranged from 1:6 to 1:16 (3,0–4,0 log2) and above.


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