{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T14:32:11Z","timestamp":1791297131857,"version":"4.1.0"},"reference-count":22,"publisher":"American Society for Microbiology","issue":"15","license":[{"start":{"date-parts":[[2014,8,1]],"date-time":"2014-08-01T00:00:00Z","timestamp":1406851200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Virol"],"published-print":{"date-parts":[[2014,8]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>Interaction between E and prM proteins in flavivirus-infected cells is a major factor for virus-like particle (VLP) production. The prM helical (prM-H) domain is topologically close to and may interact with domain II of the E protein (EDII). In this study, we investigated prM-H domain amino acid residues facing Japanese encephalitis virus EDII using site-directed mutagenesis to determine their roles in prM-E interaction and VLP production. Our results indicate that negatively charged prM-E125 residue at the prM-H domain affected VLP production via one or more interactions with positively charged E-K93 and E-H246 residues at EDII. Exchanges of oppositely charged residue side chains at prM-E125\/E-K93 and prM-E125\/E-H246 are recoverable for VLP production. The prM-E125 and E-H246 residues are conserved and that the positive charge of the E-K93 residue is preserved in different flavivirus groups. These findings suggest that the electrostatic attractions of prM-E125, E-K93, and E-H246 residues are important to flavivirus VLP production and that inhibiting these interactions is a potential strategy for blocking flavivirus infections.<\/jats:p>\n          <jats:p>\n            <jats:bold>IMPORTANCE<\/jats:bold>\n            Molecular interaction between E and prM proteins of Japanese encephalitis virus is a major driving force for virus-like particle (VLP) production. The current high-resolution structures available for prM-E complexes do not include the membrane proximal stem region of prM. The prM stem region contains an N-terminal loop and a helix domain (prM-H). Since the prM-H domain is topologically close to domain II of the E protein (EDII), this study was to determine molecular interactions between the prM-H domain and EDII. We found that the molecular interactions between prM-E125 residue and positively charged E-K93 and E-H246 residues at EDII are critical for VLP production. More importantly, the prM-E125 and E-H246 residues are conserved and the positive charge of the E-K93 residue is preserved in different flavivirus groups. Our findings help refine the structure and molecular interactions on the flavivirus surface and reveal a potential strategy for blocking flavivirus infections by inhibiting these electrostatic interactions.\n          <\/jats:p>","DOI":"10.1128\/jvi.00937-14","type":"journal-article","created":{"date-parts":[[2014,5,15]],"date-time":"2014-05-15T01:56:52Z","timestamp":1400119012000},"page":"8386-8396","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":17,"title":["Glutamic Acid at Residue 125 of the prM Helix Domain Interacts with Positively Charged Amino Acids in E Protein Domain II for Japanese Encephalitis Virus-Like-Particle Production"],"prefix":"10.1128","volume":"88","author":[{"given":"Jia-Guan","family":"Peng","sequence":"first","affiliation":[{"name":"Institute of Biotechnology, National Tsing Hua University, Hsinchu, Taiwan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Suh-Chin","family":"Wu","sequence":"additional","affiliation":[{"name":"Institute of Biotechnology, National Tsing Hua University, Hsinchu, Taiwan"},{"name":"Department of Medical Science, National Tsing Hua University, Hsinchu, Taiwan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","first-page":"1043","volume-title":"Fields virology","author":"Burke DS","year":"2001","unstructured":"BurkeDSMonathTP. 2001 Flaviviruses, p 1043\u20131125. 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