Abstract
CMVpp65, a candidate component of human cytomegalovirus (CMV) vaccines, has phosphokinase (PK) activity that could affect vaccine safety. A mutated form of CMVpp65 substituting asparagine for lysine at the adenosine triphosphate (ATP)-binding site (CMVpp65mII) is kinase-deficient. Using DNA immunizations in a transgenic human leucocyte antigen (HLA)A*0201.Kb mouse model, the mutated CMVpp65 induced cytotoxic T lymphocytes (CTL) immunity similarly to native CMVpp65. Murine CTL lines generated from these immunizations killed human cells either after sensitization with CMVpp65-specific peptides or after infection with either CMV-Towne strain or rvac-pp65. It is proposed that CMVpp65mII be evaluated in candidate vaccines for CMV.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Cells, Cultured
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Cytomegalovirus / immunology*
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Cytomegalovirus Infections / immunology*
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Cytomegalovirus Infections / prevention & control
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Epitopes, T-Lymphocyte / immunology
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Female
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HLA-A Antigens / immunology*
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Humans
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Immunization
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Mice
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Mice, Inbred C57BL
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Mice, Transgenic
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Phosphoproteins / genetics
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Phosphoproteins / immunology*
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Phosphoproteins / metabolism
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T-Lymphocytes, Cytotoxic / immunology*
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Vaccines, DNA / genetics
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Vaccines, DNA / immunology*
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Vaccinia virus / genetics
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Viral Matrix Proteins / genetics
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Viral Matrix Proteins / immunology*
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Viral Matrix Proteins / metabolism
Substances
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Epitopes, T-Lymphocyte
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HLA-A Antigens
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Phosphoproteins
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Vaccines, DNA
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Viral Matrix Proteins
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cytomegalovirus matrix protein 65kDa