Haemagglutinin (HA) and fusion (F) proteins of peste-des-petits-ruminants virus (PPRV) and rinderpest virus (RPV) were purified by immunoaffinity chromatography. The purified proteins were characterized by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS-PAGE). Rabbit hyperimmune sera were raised against the purified HA and F proteins and assayed by enzyme-linked immunosorbent assay (ELISA), haemagglutination-inhibition (HAI) and virus neutralization (VN) tests. The immunized animals were challenged with a virulent lapinized (rabbit-adapted) strain of RPV. Both HA and F proteins of PPRV protected rabbits against a lethal challenge with lapinized RPV. As expected, RPV HA and F proteins also conferred a similar protection against the homologous challenge. The postchallenge antibody responses were of a true anamnestic type.

Download full-text PDF

Source

Publication Analysis

Top Keywords

rinderpest virus
8
purified proteins
8
rpv proteins
8
proteins
5
protection rabbits
4
rabbits lapinized
4
lapinized rinderpest
4
virus
4
purified
4
virus purified
4

Similar Publications

Rinderpest and peste des petits ruminants (PPR) are two closely related viral diseases caused by viruses belonging to the genus Morbillivirus and affecting ruminants. Both diseases are notifiable to the World Organisation for Animal Health (WOAH) due to their high contagiosity and economic importance. International collaboration and scientific developments have led to the eradication of rinderpest, which was celebrated in 2011, 250 years after the first veterinary school was created in Lyon.

View Article and Find Full Text PDF

Rinderpest virus and peste des petits ruminants (PPR) virus are highly pathogenic viruses causing disease primarily in cattle and small ruminants, respectively. Although the post-eradication process for rinderpest has been largely successful, gaps in preparedness for a future rinderpest reappearance remain, and the virus is still held in some facilities that have not been registered or inspected, posing a threat to the global community. The PPR Global Eradication Programme will need to overcome significant hurdles to reach a world free of the disease by 2030.

View Article and Find Full Text PDF

Background: Peste des petits ruminants (PPR) is a viral disease that affects domestic and wild small ruminants and camels in Africa, the Middle East, and Asia. Following the successful eradication of rinderpest, the World Organization for Animal Health (WOAH) and the Food and Agriculture Organization (FAO) have undertaken to eradicate PPR by 2030. Regular surveillance and monitoring of the disease in various regions of Ethiopia are crucial to achieving this goal.

View Article and Find Full Text PDF

This review provides an overview of the canine distemper virus (CDV), a highly infectious pathogen causing severe disease in domestic dogs and wildlife. It shares genetic similarities with the human measles virus (HMV) in humans and the rinderpest virus (RPV) in cattle. The origin of CDV likely involves a mutation from human measles strains, possibly in the New World, with subsequent transmission to dogs.

View Article and Find Full Text PDF

Glycan-shielded homodimer structure and dynamical features of the canine distemper virus hemagglutinin relevant for viral entry and efficient vaccination.

Elife

July 2024

Laboratory of Biomolecular Science and Center for Research and Education on Drug Discovery, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.

Canine distemper virus (CDV) belongs to morbillivirus, including measles virus (MeV) and rinderpest virus, which causes serious immunological and neurological disorders in carnivores, including dogs and rhesus monkeys, as recently reported, but their vaccines are highly effective. The attachment glycoprotein hemagglutinin (CDV-H) at the CDV surface utilizes signaling lymphocyte activation molecule (SLAM) and Nectin-4 (also called poliovirus-receptor-like-4; PVRL4) as entry receptors. Although fusion models have been proposed, the molecular mechanism of morbillivirus fusion entry is poorly understood.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!