Inhibition of prion propagation in scrapie-infected mouse neuroblastoma cell lines using mouse monoclonal antibodies against prion protein
We screened six mouse monoclonal antibodies (mAbs) against prion protein (PrP), which were previously established in our laboratory, for inhibitory activity against PrP Sc-accumulation in scrapie-infected cell lines and identified two mAbs, 3S9 and 2H9, as possessing this inhibitory activity. mAb 3S...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2005-09, Vol.335 (1), p.197-204 |
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| creator | Miyamoto, Kazuyoshi Nakamura, Naoto Aosasa, Masayoshi Nishida, Noriyuki Yokoyama, Takashi Horiuchi, Hiroyuki Furusawa, Shuichi Matsuda, Haruo |
| description | We screened six mouse monoclonal antibodies (mAbs) against prion protein (PrP), which were previously established in our laboratory, for inhibitory activity against PrP
Sc-accumulation in scrapie-infected cell lines and identified two mAbs, 3S9 and 2H9, as possessing this inhibitory activity. mAb 3S9 recognized an epitope including 154th tyrosine in the helix 1 region of PrP, while mAb 2H9 recognized a discontinuous region that included helix 1. In three scrapie-infected cell lines infected with different mouse-adapted scrapie strains, mAb 3S9 strongly inhibited accumulation of PrP
Sc, while mAb 2H9 moderately inhibited accumulation of PrP
Sc, indicating that inhibition of prion propagation by mAbs may be dependent on PrP
Sc characteristics. Furthermore, mAb 3S9 completely excluded PrP
Sc from these cell lines. These results suggest that mAbs 3S9 and 2H9 might be useful for clarifying the mechanisms of prion propagation and prevention by PrP-specific antibodies, and for tracing the conversion of PrP
C to other PrP
Sc isoforms. |
| doi_str_mv | 10.1016/j.bbrc.2005.07.063 |
| format | Article |
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Sc-accumulation in scrapie-infected cell lines and identified two mAbs, 3S9 and 2H9, as possessing this inhibitory activity. mAb 3S9 recognized an epitope including 154th tyrosine in the helix 1 region of PrP, while mAb 2H9 recognized a discontinuous region that included helix 1. In three scrapie-infected cell lines infected with different mouse-adapted scrapie strains, mAb 3S9 strongly inhibited accumulation of PrP
Sc, while mAb 2H9 moderately inhibited accumulation of PrP
Sc, indicating that inhibition of prion propagation by mAbs may be dependent on PrP
Sc characteristics. Furthermore, mAb 3S9 completely excluded PrP
Sc from these cell lines. These results suggest that mAbs 3S9 and 2H9 might be useful for clarifying the mechanisms of prion propagation and prevention by PrP-specific antibodies, and for tracing the conversion of PrP
C to other PrP
Sc isoforms.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2005.07.063</identifier><identifier>PMID: 16061207</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>154th tyrosine of PrP ; Amino Acid Sequence ; Animals ; Antibodies, Monoclonal - immunology ; Antibodies, Monoclonal - pharmacology ; Antibody Specificity ; Cell Line ; Endopeptidase K - metabolism ; Epitopes - chemistry ; Epitopes - immunology ; Helix 1 of PrP ; Humans ; Inhibition of prion accumulation ; Mice ; Molecular Sequence Data ; Neuroblastoma - immunology ; Neuroblastoma - metabolism ; Neuroblastoma - pathology ; Prion strain ; Prions - chemistry ; Prions - immunology ; Prions - metabolism ; PrP-specific antibody ; Scrapie - immunology ; Scrapie - metabolism ; Scrapie - pathology ; Sequence Alignment</subject><ispartof>Biochemical and biophysical research communications, 2005-09, Vol.335 (1), p.197-204</ispartof><rights>2005 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c451t-c08ac19cf9fbe1b03c1fa6111393cd31840d508389bfef3bc234557dc9153e923</citedby><cites>FETCH-LOGICAL-c451t-c08ac19cf9fbe1b03c1fa6111393cd31840d508389bfef3bc234557dc9153e923</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X05015421$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16061207$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Miyamoto, Kazuyoshi</creatorcontrib><creatorcontrib>Nakamura, Naoto</creatorcontrib><creatorcontrib>Aosasa, Masayoshi</creatorcontrib><creatorcontrib>Nishida, Noriyuki</creatorcontrib><creatorcontrib>Yokoyama, Takashi</creatorcontrib><creatorcontrib>Horiuchi, Hiroyuki</creatorcontrib><creatorcontrib>Furusawa, Shuichi</creatorcontrib><creatorcontrib>Matsuda, Haruo</creatorcontrib><title>Inhibition of prion propagation in scrapie-infected mouse neuroblastoma cell lines using mouse monoclonal antibodies against prion protein</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>We screened six mouse monoclonal antibodies (mAbs) against prion protein (PrP), which were previously established in our laboratory, for inhibitory activity against PrP
Sc-accumulation in scrapie-infected cell lines and identified two mAbs, 3S9 and 2H9, as possessing this inhibitory activity. mAb 3S9 recognized an epitope including 154th tyrosine in the helix 1 region of PrP, while mAb 2H9 recognized a discontinuous region that included helix 1. In three scrapie-infected cell lines infected with different mouse-adapted scrapie strains, mAb 3S9 strongly inhibited accumulation of PrP
Sc, while mAb 2H9 moderately inhibited accumulation of PrP
Sc, indicating that inhibition of prion propagation by mAbs may be dependent on PrP
Sc characteristics. Furthermore, mAb 3S9 completely excluded PrP
Sc from these cell lines. These results suggest that mAbs 3S9 and 2H9 might be useful for clarifying the mechanisms of prion propagation and prevention by PrP-specific antibodies, and for tracing the conversion of PrP
C to other PrP
Sc isoforms.</description><subject>154th tyrosine of PrP</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Antibodies, Monoclonal - pharmacology</subject><subject>Antibody Specificity</subject><subject>Cell Line</subject><subject>Endopeptidase K - metabolism</subject><subject>Epitopes - chemistry</subject><subject>Epitopes - immunology</subject><subject>Helix 1 of PrP</subject><subject>Humans</subject><subject>Inhibition of prion accumulation</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Neuroblastoma - immunology</subject><subject>Neuroblastoma - metabolism</subject><subject>Neuroblastoma - pathology</subject><subject>Prion strain</subject><subject>Prions - chemistry</subject><subject>Prions - immunology</subject><subject>Prions - metabolism</subject><subject>PrP-specific antibody</subject><subject>Scrapie - immunology</subject><subject>Scrapie - metabolism</subject><subject>Scrapie - pathology</subject><subject>Sequence Alignment</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcuKFTEQhoMoznH0BVxIVu66rer0LeBGBi8DA24U3IUkXRlz6E6OSbfgK_jUpj0HZqerhPDVX1X5GHuJUCNg_-ZYG5Ns3QB0NQw19OIROyBIqBqE9jE7AEBfNRK_XbFnOR8BENtePmVX2EOPDQwH9vs2fPfGrz4GHh0_pf1ySvGk7_XfRx94tkmfPFU-OLIrTXyJWyYeaEvRzDqvcdHc0jzz2QfKfMs-3F-gJYZo5xj0zHVYvYmTL0QJ9yGvD-1W8uE5e-L0nOnF5bxmXz-8_3Lzqbr7_PH25t1dZdsO18rCqC1K66QzhAaERad7RBRS2Eng2MLUwShGaRw5YWwj2q4bJiuxEyQbcc1en3NL3x8b5VUtPu_j60BlZtWP7Th2A_4XxEHIUUpZwOYM2hRzTuRUWWzR6ZdCULsqdVS7KrWrUjCooqoUvbqkb2ah6aHk4qYAb88Alc_46SmpbD0FS5NPxYOaov9X_h-CMqip</recordid><startdate>20050916</startdate><enddate>20050916</enddate><creator>Miyamoto, Kazuyoshi</creator><creator>Nakamura, Naoto</creator><creator>Aosasa, Masayoshi</creator><creator>Nishida, Noriyuki</creator><creator>Yokoyama, Takashi</creator><creator>Horiuchi, Hiroyuki</creator><creator>Furusawa, Shuichi</creator><creator>Matsuda, Haruo</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TK</scope><scope>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20050916</creationdate><title>Inhibition of prion propagation in scrapie-infected mouse neuroblastoma cell lines using mouse monoclonal antibodies against prion protein</title><author>Miyamoto, Kazuyoshi ; Nakamura, Naoto ; Aosasa, Masayoshi ; Nishida, Noriyuki ; Yokoyama, Takashi ; Horiuchi, Hiroyuki ; Furusawa, Shuichi ; Matsuda, Haruo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c451t-c08ac19cf9fbe1b03c1fa6111393cd31840d508389bfef3bc234557dc9153e923</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>154th tyrosine of PrP</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Antibodies, Monoclonal - pharmacology</topic><topic>Antibody Specificity</topic><topic>Cell Line</topic><topic>Endopeptidase K - metabolism</topic><topic>Epitopes - chemistry</topic><topic>Epitopes - immunology</topic><topic>Helix 1 of PrP</topic><topic>Humans</topic><topic>Inhibition of prion accumulation</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Neuroblastoma - immunology</topic><topic>Neuroblastoma - metabolism</topic><topic>Neuroblastoma - pathology</topic><topic>Prion strain</topic><topic>Prions - chemistry</topic><topic>Prions - immunology</topic><topic>Prions - metabolism</topic><topic>PrP-specific antibody</topic><topic>Scrapie - immunology</topic><topic>Scrapie - metabolism</topic><topic>Scrapie - pathology</topic><topic>Sequence Alignment</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Miyamoto, Kazuyoshi</creatorcontrib><creatorcontrib>Nakamura, Naoto</creatorcontrib><creatorcontrib>Aosasa, Masayoshi</creatorcontrib><creatorcontrib>Nishida, Noriyuki</creatorcontrib><creatorcontrib>Yokoyama, Takashi</creatorcontrib><creatorcontrib>Horiuchi, Hiroyuki</creatorcontrib><creatorcontrib>Furusawa, Shuichi</creatorcontrib><creatorcontrib>Matsuda, Haruo</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Miyamoto, Kazuyoshi</au><au>Nakamura, Naoto</au><au>Aosasa, Masayoshi</au><au>Nishida, Noriyuki</au><au>Yokoyama, Takashi</au><au>Horiuchi, Hiroyuki</au><au>Furusawa, Shuichi</au><au>Matsuda, Haruo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Inhibition of prion propagation in scrapie-infected mouse neuroblastoma cell lines using mouse monoclonal antibodies against prion protein</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2005-09-16</date><risdate>2005</risdate><volume>335</volume><issue>1</issue><spage>197</spage><epage>204</epage><pages>197-204</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>We screened six mouse monoclonal antibodies (mAbs) against prion protein (PrP), which were previously established in our laboratory, for inhibitory activity against PrP
Sc-accumulation in scrapie-infected cell lines and identified two mAbs, 3S9 and 2H9, as possessing this inhibitory activity. mAb 3S9 recognized an epitope including 154th tyrosine in the helix 1 region of PrP, while mAb 2H9 recognized a discontinuous region that included helix 1. In three scrapie-infected cell lines infected with different mouse-adapted scrapie strains, mAb 3S9 strongly inhibited accumulation of PrP
Sc, while mAb 2H9 moderately inhibited accumulation of PrP
Sc, indicating that inhibition of prion propagation by mAbs may be dependent on PrP
Sc characteristics. Furthermore, mAb 3S9 completely excluded PrP
Sc from these cell lines. These results suggest that mAbs 3S9 and 2H9 might be useful for clarifying the mechanisms of prion propagation and prevention by PrP-specific antibodies, and for tracing the conversion of PrP
C to other PrP
Sc isoforms.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16061207</pmid><doi>10.1016/j.bbrc.2005.07.063</doi><tpages>8</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 2005-09, Vol.335 (1), p.197-204 |
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| subjects | 154th tyrosine of PrP Amino Acid Sequence Animals Antibodies, Monoclonal - immunology Antibodies, Monoclonal - pharmacology Antibody Specificity Cell Line Endopeptidase K - metabolism Epitopes - chemistry Epitopes - immunology Helix 1 of PrP Humans Inhibition of prion accumulation Mice Molecular Sequence Data Neuroblastoma - immunology Neuroblastoma - metabolism Neuroblastoma - pathology Prion strain Prions - chemistry Prions - immunology Prions - metabolism PrP-specific antibody Scrapie - immunology Scrapie - metabolism Scrapie - pathology Sequence Alignment |
| title | Inhibition of prion propagation in scrapie-infected mouse neuroblastoma cell lines using mouse monoclonal antibodies against prion protein |
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