Matches in SemOpenAlex for { <https://semopenalex.org/work/W2094529805> ?p ?o ?g. }
- W2094529805 endingPage "471" @default.
- W2094529805 startingPage "461" @default.
- W2094529805 abstract "The nature of the initial interactions of African swine fever (ASF) virus with target cells is only partially known, and to date only the ASF virus protein p12 has been identified as a viral attachment protein. More recently, antibodies to viral proteins p54 and p30 have been shown to neutralize the virus, inhibiting virus binding and internalization, respectively. Therefore, we investigated the role of these proteins in the receptor-mediated ASF virus endocytosis in swine macrophages, the natural host cells. Proteins p54 and p30, released from ASF virus particles after treatment of virions with a nonionic detergent, bound to virus-sensitive alveolar pig macrophages. Binding of these proteins was found to be specifically inhibited by neutralizing antibodies obtained from a convalescent pig or from pigs immunized with recombinant p54 or p30 proteins. The baculovirus-expressed proteins p54 and p30 retained the same biological properties as the viral proteins, since they also bound specifically to these cells, and their binding was equally inhibited by neutralizing antibodies. Binding of 35S-labeled recombinant p54 and p30 proteins to macrophages was specifically competed by an excess of unlabeled p54 and p30, respectively. However, cross-binding inhibition was not observed, suggesting the existence of two different saturable binding sites for these proteins in the susceptible cells. In addition, protein p54 blocked the specific binding of virus particles to the macrophage, while protein p30 blocked virus internalization. Both proteins independently prevented virus infection and in a dose-dependent manner, suggesting that binding interactions mediated by both proteins are necessary to give rise to a productive infection. The relevance of blockade of virus-cell interactions mediated by p54 and p30 in the protective immune response against ASF virus was then investigated. Immunization of pigs with either recombinant p54 or p30 proteins induced neutralizing antibodies which, as expected, inhibited virus attachment or internalization, respectively. However, immunized pigs were not protected against lethal infection and the disease course was not modified in these animals. In contrast, immunization with a combination of p54 and p30 proteins simultaneously stimulated both virus neutralizing mechanisms and modified drastically the disease course, rendering a variable degree of protection ranging from a delay in the onset of the disease to complete protection against virus infection. In conclusion, the above results strongly suggest that proteins p54 and p30 mediate specific interactions between ASF virus and cellular receptors and that simultaneous interference with these two interactions has a complementary effect in antibody-mediated protection." @default.
- W2094529805 created "2016-06-24" @default.
- W2094529805 creator A5007364208 @default.
- W2094529805 creator A5026998248 @default.
- W2094529805 creator A5048087932 @default.
- W2094529805 creator A5057417720 @default.
- W2094529805 creator A5061201501 @default.
- W2094529805 creator A5069152749 @default.
- W2094529805 date "1998-04-01" @default.
- W2094529805 modified "2023-10-18" @default.
- W2094529805 title "The African Swine Fever Virus Proteins p54 and p30 Are Involved in Two Distinct Steps of Virus Attachment and Both Contribute to the Antibody-Mediated Protective Immune Response" @default.
- W2094529805 cites W11304378 @default.
- W2094529805 cites W1545152378 @default.
- W2094529805 cites W1570685643 @default.
- W2094529805 cites W1578860231 @default.
- W2094529805 cites W1580939688 @default.
- W2094529805 cites W1857660355 @default.
- W2094529805 cites W1964016573 @default.
- W2094529805 cites W1970412419 @default.
- W2094529805 cites W1986768688 @default.
- W2094529805 cites W2007881500 @default.
- W2094529805 cites W2011602486 @default.
- W2094529805 cites W2014971990 @default.
- W2094529805 cites W2017019498 @default.
- W2094529805 cites W2018124147 @default.
- W2094529805 cites W2025300828 @default.
- W2094529805 cites W2031183047 @default.
- W2094529805 cites W2032371793 @default.
- W2094529805 cites W2034389832 @default.
- W2094529805 cites W2045526919 @default.
- W2094529805 cites W2047097950 @default.
- W2094529805 cites W2058074887 @default.
- W2094529805 cites W2069990125 @default.
- W2094529805 cites W2083006593 @default.
- W2094529805 cites W2087601007 @default.
- W2094529805 cites W2091474834 @default.
- W2094529805 cites W2092923090 @default.
- W2094529805 cites W2099887596 @default.
- W2094529805 cites W2147653501 @default.
- W2094529805 cites W2162976896 @default.
- W2094529805 cites W2911280876 @default.
- W2094529805 cites W54799168 @default.
- W2094529805 doi "https://doi.org/10.1006/viro.1998.9068" @default.
- W2094529805 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9568043" @default.
- W2094529805 hasPublicationYear "1998" @default.
- W2094529805 type Work @default.
- W2094529805 sameAs 2094529805 @default.
- W2094529805 citedByCount "165" @default.
- W2094529805 countsByYear W20945298052012 @default.
- W2094529805 countsByYear W20945298052013 @default.
- W2094529805 countsByYear W20945298052014 @default.
- W2094529805 countsByYear W20945298052015 @default.
- W2094529805 countsByYear W20945298052016 @default.
- W2094529805 countsByYear W20945298052017 @default.
- W2094529805 countsByYear W20945298052018 @default.
- W2094529805 countsByYear W20945298052019 @default.
- W2094529805 countsByYear W20945298052020 @default.
- W2094529805 countsByYear W20945298052021 @default.
- W2094529805 countsByYear W20945298052022 @default.
- W2094529805 countsByYear W20945298052023 @default.
- W2094529805 crossrefType "journal-article" @default.
- W2094529805 hasAuthorship W2094529805A5007364208 @default.
- W2094529805 hasAuthorship W2094529805A5026998248 @default.
- W2094529805 hasAuthorship W2094529805A5048087932 @default.
- W2094529805 hasAuthorship W2094529805A5057417720 @default.
- W2094529805 hasAuthorship W2094529805A5061201501 @default.
- W2094529805 hasAuthorship W2094529805A5069152749 @default.
- W2094529805 hasBestOaLocation W20945298051 @default.
- W2094529805 hasConcept C104317684 @default.
- W2094529805 hasConcept C139770010 @default.
- W2094529805 hasConcept C140704245 @default.
- W2094529805 hasConcept C153911025 @default.
- W2094529805 hasConcept C159047783 @default.
- W2094529805 hasConcept C159654299 @default.
- W2094529805 hasConcept C170493617 @default.
- W2094529805 hasConcept C196594336 @default.
- W2094529805 hasConcept C203014093 @default.
- W2094529805 hasConcept C2522874641 @default.
- W2094529805 hasConcept C2778359420 @default.
- W2094529805 hasConcept C28005876 @default.
- W2094529805 hasConcept C40767141 @default.
- W2094529805 hasConcept C55493867 @default.
- W2094529805 hasConcept C58475186 @default.
- W2094529805 hasConcept C86295872 @default.
- W2094529805 hasConcept C86803240 @default.
- W2094529805 hasConceptScore W2094529805C104317684 @default.
- W2094529805 hasConceptScore W2094529805C139770010 @default.
- W2094529805 hasConceptScore W2094529805C140704245 @default.
- W2094529805 hasConceptScore W2094529805C153911025 @default.
- W2094529805 hasConceptScore W2094529805C159047783 @default.
- W2094529805 hasConceptScore W2094529805C159654299 @default.
- W2094529805 hasConceptScore W2094529805C170493617 @default.
- W2094529805 hasConceptScore W2094529805C196594336 @default.
- W2094529805 hasConceptScore W2094529805C203014093 @default.
- W2094529805 hasConceptScore W2094529805C2522874641 @default.
- W2094529805 hasConceptScore W2094529805C2778359420 @default.
- W2094529805 hasConceptScore W2094529805C28005876 @default.
- W2094529805 hasConceptScore W2094529805C40767141 @default.