Selected article for: "cell fusion and monoclonal antibody"
Author: Miyoshi-Akiyama, Tohru; Ishida, Isao; Fukushi, Masaya; Yamaguchi, Keina; Matsuoka, Yusuke; Ishihara, Takashi; Tsukahara, Masayoshi; Hatakeyama, Seisuke; Itoh, Norikazu; Morisawa, Aki; Yoshinaka, Yoshiyuki; Yamamoto, Naoki; Lianfeng, Zhang; Chuan, Qin; Kirikae, Teruo; Sasazuki, Takehiko
Title: Fully Human Monoclonal Antibody Directed to Proteolytic Cleavage Site in Severe Acute Respiratory Syndrome (SARS) Coronavirus S Protein Neutralizes the Virus in a Rhesus Macaque SARS Model
  • Cord-id: kv3363qh
  • Document date: 2011_6_1
    • ID: kv3363qh
    Snippet: Background. There is still no effective method to prevent or treat severe acute respiratory syndrome (SARS), which is caused by SARS coronavirus (CoV). In the present study, we evaluated the efficacy of a fully human monoclonal antibody capable of neutralizing SARS-CoV in vitro in a Rhesus macaque model of SARS. Methods. The antibody 5H10 was obtained by vaccination of KM mice bearing human immunoglobulin genes with Escherichiacoli–producing recombinant peptide containing the dominant epitope
    Document: Background. There is still no effective method to prevent or treat severe acute respiratory syndrome (SARS), which is caused by SARS coronavirus (CoV). In the present study, we evaluated the efficacy of a fully human monoclonal antibody capable of neutralizing SARS-CoV in vitro in a Rhesus macaque model of SARS. Methods. The antibody 5H10 was obtained by vaccination of KM mice bearing human immunoglobulin genes with Escherichiacoli–producing recombinant peptide containing the dominant epitope of the viral spike protein found in convalescent serum samples from patients with SARS. Results. 5H10, which recognized the same epitope that is also a cleavage site critical for the entry of SARS-CoV into host cells, inhibited propagation of the virus and pathological changes found in Rhesus macaques infected with the virus through the nasal route. In addition, we analyzed the mode of action of 5H10, and the results suggested that 5H10 inhibited fusion between the virus envelope and host cell membrane. 5H10 has potential for use in prevention and treatment of SARS if it reemerges. Conclusions. This study represents a platform to produce fully human antibodies against emerging infectious diseases in a timely and safe manner.

    Search related documents:
    Co phrase search for related documents
    • absence presence and administration group: 1, 2
    • absence presence and luciferase activity: 1, 2, 3, 4, 5
    • absence presence and lung damage: 1, 2
    • acetic acid and acid alcohol: 1
    • acetic acid and lung damage: 1
    • acute dad diffuse alveolar damage and lung damage: 1, 2, 3, 4, 5
    • acute respiratory syndrome and additional fragment: 1, 2
    • acute respiratory syndrome and administration group: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15
    • acute respiratory syndrome and luciferase activity: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18
    • acute respiratory syndrome and lung damage: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25
    • acute respiratory syndrome and lung damage severity: 1, 2, 3, 4, 5, 6, 7, 8, 9
    • administration group and lung damage: 1, 2