title: Cellular Prion Protein Combined with Galectin-3 and -6 Affects the Infectivity Titer of an Endogenous Retrovirus Assayed in Hippocampal Neuronal Cells.
abstract: Prion diseases are infectious and fatal neurodegenerative diseases which require the cellular prion protein, PrPC, for development of diseases. The current study shows that the PrPC augments infectivity and plaque formation of a mouse endogenous retrovirus, MuLV. We have established four neuronal cell lines expressing mouse PrPC, PrP+/+; two express wild type PrPC (MoPrPwild) and the other two express mutant PrPC (MoPrPmut). Infection of neuronal cells from various PrP+/+ and PrP-/- (MoPrPKO) lines with MuLV yielded at least three times as many plaques in PrP+/+ than in PrP-/-. Furthermore, among the four PrP+/+ lines, one mutant line, P101L, had at least 2.5 times as many plaques as the other three PrP+/+ lines. Plaques in P101L were four times larger than those in other PrP+/+ lines. Colocalization of PrP and CAgag was seen in MuLV-infected PrP+/+ cells. In the PrP-MuLV interaction, the involvement of galectin-3 and -6 was observed by immunoprecipitation with antibody to PrPC. These results suggest that PrPC combined with galectin-3 and -6 can act as a receptor for MuLV. P101L, the disease form of mutant PrPC results suggest the genetic mutant form of PrPC may be more susceptible to viral infection.
authors.affiliation: Department of Medicine, Division of Infectious Diseases, Icahn School of Medicine at Mount Sinai, New York, New York, United States of America.
authors.forename: Boe-Hyun
authors.identifier: http://orcid.org/0000-0003-2821-0467
authors.initials: BH
authors.lastname: Kim
authors.affiliation: Ilsong Institute of Life Science, Hallym University, Gwanyang-dong, Dongan-gu, Anyang, Gyeonggi-do, Republic of Korea.
authors.forename: Hae-Young
authors.initials: HY
authors.lastname: Shin
authors.affiliation: Department of Chemistry, California State University, Fresno, California, United States of America.
authors.forename: Joy J
authors.initials: JJ
authors.lastname: Goto
authors.affiliation: New York State Institute for Basic Research in Developmental Disabilities, Staten Island, New York, United States of America.
authors.forename: Richard I
authors.initials: RI
authors.lastname: Carp
authors.affiliation: Ilsong Institute of Life Science, Hallym University, Gwanyang-dong, Dongan-gu, Anyang, Gyeonggi-do, Republic of Korea.
authors.forename: Eun-Kyoung
authors.initials: EK
authors.lastname: Choi
authors.affiliation: Ilsong Institute of Life Science, Hallym University, Gwanyang-dong, Dongan-gu, Anyang, Gyeonggi-do, Republic of Korea.
authors.forename: Yong-Sun
authors.initials: YS
authors.lastname: Kim
mesh_terms: D000818:Animals; D000831:Animals, Newborn; D001253:Astrocytes / Q000166:cytology / Q000378:metabolism / Q000821:virology; D015153:Blotting, Western; D002460:Cell Line; D002478:Cells, Cultured; D020077:Endogenous Retroviruses / Q000254:growth & development / Q000502:physiology; D037502:Galectin 3 / Q000235:genetics / Q000378:metabolism*; D037161:Galectins / Q000235:genetics / Q000378:metabolism*; D006624:Hippocampus / Q000166:cytology / Q000821:virology; D054884:Host-Pathogen Interactions; D009052:Leukemia Virus, Murine / Q000254:growth & development* / Q000502:physiology; D018345:Mice, Knockout; D018613:Microscopy, Confocal; D009474:Neurons / Q000166:cytology / Q000378:metabolism* / Q000821:virology; D018621:PrPC Proteins / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D020133:Reverse Transcriptase Polymerase Chain Reaction
chemical_list: D037502:Galectin 3; D037161:Galectins; C110383:Lgals6 protein, mouse; D018621:PrPC Proteins