Development and Characterization of an Oncolytic Human Adenovirus-Based Vector Co-Expressing the Adenovirus Death Protein and p14 Fusion-Associated Small Transmembrane Fusogenic Protein
Human adenovirus (HAdV)-based oncolytic vectors, which are designed to preferentially replicate in and kill cancer cells, have shown modest efficacy in human clinical trials in part due to poor viral distribution throughout the tumor mass. Previously, we showed that expression of the p14 fusion-asso...
Gespeichert in:
Veröffentlicht in: | International journal of molecular sciences 2024-11, Vol.25 (22), p.12451 |
---|---|
Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | |
---|---|
container_issue | 22 |
container_start_page | 12451 |
container_title | International journal of molecular sciences |
container_volume | 25 |
creator | Poulin, Kathy L Clarkin, Ryan G Del Papa, Joshua Parks, Robin J |
description | Human adenovirus (HAdV)-based oncolytic vectors, which are designed to preferentially replicate in and kill cancer cells, have shown modest efficacy in human clinical trials in part due to poor viral distribution throughout the tumor mass. Previously, we showed that expression of the p14 fusion-associated small transmembrane (FAST) fusogenic protein could enhance oncolytic HAdV efficacy and reduce tumor growth rate in a human xenograft mouse model of cancer. We now explore whether co-expression of the adenovirus death protein (ADP) with p14 FAST protein could synergize to further enhance oncolytic vector efficacy. ADP is naturally encoded within the early region 3 (E3) of HAdV, a region which is frequently removed from HAdV-based vectors, and functions to enhance cell lysis and progeny release. We evaluated a variety of approaches to achieve optimal expression of the two proteins, the most efficient method being insertion of an expression cassette within the E3 deletion, consisting of the coding sequences for p14 FAST protein and ADP separated by a self-cleaving peptide derived from the porcine teschovirus-1 (P2A). However, the quantities of p14 FAST protein and ADP produced from this vector were reduced approximately 10-fold compared to a similar vector-expressing only p14 FAST protein and wildtype HAdV, respectively. Compared to our original oncolytic vector-expressing p14 FAST protein alone, reduced expression of p14 FAST protein and ADP from the P2A construct reduced cell-cell fusion, vector spread, and cell-killing activity in human A549 adenocarcinoma cells in culture. These studies show that a self-cleaving peptide can be used to express two different transgenes in an armed oncolytic HAdV vector, but also highlight the challenges in maintaining adequate transgene expression when modifying vector design. |
doi_str_mv | 10.3390/ijms252212451 |
format | Article |
fullrecord | <record><control><sourceid>gale_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_11594305</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A818337876</galeid><sourcerecordid>A818337876</sourcerecordid><originalsourceid>FETCH-LOGICAL-c330t-e224da878ec78455b091d3884555d1be4cae01e4ee9cb573f439b9da2643c1b03</originalsourceid><addsrcrecordid>eNpdksFu1DAQhiMEoqVw5IosceESsD32Jjmh7balSJWKROFqOc5k16vEXmxnRXkz3g5vu5QtpxmPP___jDVF8ZrR9wAN_WDXY-SSc8aFZE-KYyY4LymdVU8P8qPiRYxrSjlw2TwvjqCRzUwyeVz8PsMtDn4zoktEu44sVjpokzDYXzpZ74jvc51cO-OH22QNuZzGfJ536PzWhimWpzpiR76jST6QhS_Pf24CxmjdkqQVHpDkDHVakS_BJ7Tuzm3DBLmYYvYp5zF6Y3XKWl9HPQzkJmgXRxzbHHFH-SW63MD-_cviWa-HiK_28aT4dnF-s7gsr64_fV7Mr0oDQFOJnItO11WNpqqFlC1tWAf1LpUda1EYjZShQGxMKyvoBTRt02k-E2BYS-Gk-Hivu5naETuTPyroQW2CHXW4VV5b9fjG2ZVa-q1iTDYCqMwK7_YKwf-YMCY12mhwGPJcfooKGICQVUXrjL79D137Kbg83x1F67oC-Ect9YDKut5nY7MTVfOa1QBVXc0yVd5TJvgYA_YPPTOqdrujHu1O5t8cDvpA_10W-AM1AsLP</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>3133088733</pqid></control><display><type>article</type><title>Development and Characterization of an Oncolytic Human Adenovirus-Based Vector Co-Expressing the Adenovirus Death Protein and p14 Fusion-Associated Small Transmembrane Fusogenic Protein</title><source>MDPI - Multidisciplinary Digital Publishing Institute</source><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><creator>Poulin, Kathy L ; Clarkin, Ryan G ; Del Papa, Joshua ; Parks, Robin J</creator><creatorcontrib>Poulin, Kathy L ; Clarkin, Ryan G ; Del Papa, Joshua ; Parks, Robin J</creatorcontrib><description>Human adenovirus (HAdV)-based oncolytic vectors, which are designed to preferentially replicate in and kill cancer cells, have shown modest efficacy in human clinical trials in part due to poor viral distribution throughout the tumor mass. Previously, we showed that expression of the p14 fusion-associated small transmembrane (FAST) fusogenic protein could enhance oncolytic HAdV efficacy and reduce tumor growth rate in a human xenograft mouse model of cancer. We now explore whether co-expression of the adenovirus death protein (ADP) with p14 FAST protein could synergize to further enhance oncolytic vector efficacy. ADP is naturally encoded within the early region 3 (E3) of HAdV, a region which is frequently removed from HAdV-based vectors, and functions to enhance cell lysis and progeny release. We evaluated a variety of approaches to achieve optimal expression of the two proteins, the most efficient method being insertion of an expression cassette within the E3 deletion, consisting of the coding sequences for p14 FAST protein and ADP separated by a self-cleaving peptide derived from the porcine teschovirus-1 (P2A). However, the quantities of p14 FAST protein and ADP produced from this vector were reduced approximately 10-fold compared to a similar vector-expressing only p14 FAST protein and wildtype HAdV, respectively. Compared to our original oncolytic vector-expressing p14 FAST protein alone, reduced expression of p14 FAST protein and ADP from the P2A construct reduced cell-cell fusion, vector spread, and cell-killing activity in human A549 adenocarcinoma cells in culture. These studies show that a self-cleaving peptide can be used to express two different transgenes in an armed oncolytic HAdV vector, but also highlight the challenges in maintaining adequate transgene expression when modifying vector design.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms252212451</identifier><identifier>PMID: 39596515</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>A549 Cells ; Adenovirus E3 Proteins ; Adenoviruses ; Adenoviruses, Human - genetics ; Analysis ; Animals ; Apoptosis ; Cancer ; Care and treatment ; Cell death ; Cell Line, Tumor ; Control ; Diagnosis ; Gene expression ; Genetic Vectors - genetics ; Humans ; Identification and classification ; Infections ; Metabolism ; Mice ; Oncolytic Virotherapy - methods ; Oncolytic Viruses - genetics ; Proteins ; Risk factors ; Viral Proteins - genetics ; Viral Proteins - metabolism ; Virus Replication - genetics ; Viruses ; Xenograft Model Antitumor Assays</subject><ispartof>International journal of molecular sciences, 2024-11, Vol.25 (22), p.12451</ispartof><rights>COPYRIGHT 2024 MDPI AG</rights><rights>2024 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2024 by the authors. 2024</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c330t-e224da878ec78455b091d3884555d1be4cae01e4ee9cb573f439b9da2643c1b03</cites><orcidid>0000-0003-2391-1010 ; 0000-0002-8420-8903</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11594305/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11594305/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/39596515$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Poulin, Kathy L</creatorcontrib><creatorcontrib>Clarkin, Ryan G</creatorcontrib><creatorcontrib>Del Papa, Joshua</creatorcontrib><creatorcontrib>Parks, Robin J</creatorcontrib><title>Development and Characterization of an Oncolytic Human Adenovirus-Based Vector Co-Expressing the Adenovirus Death Protein and p14 Fusion-Associated Small Transmembrane Fusogenic Protein</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><description>Human adenovirus (HAdV)-based oncolytic vectors, which are designed to preferentially replicate in and kill cancer cells, have shown modest efficacy in human clinical trials in part due to poor viral distribution throughout the tumor mass. Previously, we showed that expression of the p14 fusion-associated small transmembrane (FAST) fusogenic protein could enhance oncolytic HAdV efficacy and reduce tumor growth rate in a human xenograft mouse model of cancer. We now explore whether co-expression of the adenovirus death protein (ADP) with p14 FAST protein could synergize to further enhance oncolytic vector efficacy. ADP is naturally encoded within the early region 3 (E3) of HAdV, a region which is frequently removed from HAdV-based vectors, and functions to enhance cell lysis and progeny release. We evaluated a variety of approaches to achieve optimal expression of the two proteins, the most efficient method being insertion of an expression cassette within the E3 deletion, consisting of the coding sequences for p14 FAST protein and ADP separated by a self-cleaving peptide derived from the porcine teschovirus-1 (P2A). However, the quantities of p14 FAST protein and ADP produced from this vector were reduced approximately 10-fold compared to a similar vector-expressing only p14 FAST protein and wildtype HAdV, respectively. Compared to our original oncolytic vector-expressing p14 FAST protein alone, reduced expression of p14 FAST protein and ADP from the P2A construct reduced cell-cell fusion, vector spread, and cell-killing activity in human A549 adenocarcinoma cells in culture. These studies show that a self-cleaving peptide can be used to express two different transgenes in an armed oncolytic HAdV vector, but also highlight the challenges in maintaining adequate transgene expression when modifying vector design.</description><subject>A549 Cells</subject><subject>Adenovirus E3 Proteins</subject><subject>Adenoviruses</subject><subject>Adenoviruses, Human - genetics</subject><subject>Analysis</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Cancer</subject><subject>Care and treatment</subject><subject>Cell death</subject><subject>Cell Line, Tumor</subject><subject>Control</subject><subject>Diagnosis</subject><subject>Gene expression</subject><subject>Genetic Vectors - genetics</subject><subject>Humans</subject><subject>Identification and classification</subject><subject>Infections</subject><subject>Metabolism</subject><subject>Mice</subject><subject>Oncolytic Virotherapy - methods</subject><subject>Oncolytic Viruses - genetics</subject><subject>Proteins</subject><subject>Risk factors</subject><subject>Viral Proteins - genetics</subject><subject>Viral Proteins - metabolism</subject><subject>Virus Replication - genetics</subject><subject>Viruses</subject><subject>Xenograft Model Antitumor Assays</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdksFu1DAQhiMEoqVw5IosceESsD32Jjmh7balSJWKROFqOc5k16vEXmxnRXkz3g5vu5QtpxmPP___jDVF8ZrR9wAN_WDXY-SSc8aFZE-KYyY4LymdVU8P8qPiRYxrSjlw2TwvjqCRzUwyeVz8PsMtDn4zoktEu44sVjpokzDYXzpZ74jvc51cO-OH22QNuZzGfJ536PzWhimWpzpiR76jST6QhS_Pf24CxmjdkqQVHpDkDHVakS_BJ7Tuzm3DBLmYYvYp5zF6Y3XKWl9HPQzkJmgXRxzbHHFH-SW63MD-_cviWa-HiK_28aT4dnF-s7gsr64_fV7Mr0oDQFOJnItO11WNpqqFlC1tWAf1LpUda1EYjZShQGxMKyvoBTRt02k-E2BYS-Gk-Hivu5naETuTPyroQW2CHXW4VV5b9fjG2ZVa-q1iTDYCqMwK7_YKwf-YMCY12mhwGPJcfooKGICQVUXrjL79D137Kbg83x1F67oC-Ect9YDKut5nY7MTVfOa1QBVXc0yVd5TJvgYA_YPPTOqdrujHu1O5t8cDvpA_10W-AM1AsLP</recordid><startdate>20241120</startdate><enddate>20241120</enddate><creator>Poulin, Kathy L</creator><creator>Clarkin, Ryan G</creator><creator>Del Papa, Joshua</creator><creator>Parks, Robin J</creator><general>MDPI AG</general><general>MDPI</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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PHGZM</scope><scope>PHGZT</scope><scope>PIMPY</scope><scope>PJZUB</scope><scope>PKEHL</scope><scope>PPXIY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-2391-1010</orcidid><orcidid>https://orcid.org/0000-0002-8420-8903</orcidid></search><sort><creationdate>20241120</creationdate><title>Development and Characterization of an Oncolytic Human Adenovirus-Based Vector Co-Expressing the Adenovirus Death Protein and p14 Fusion-Associated Small Transmembrane Fusogenic Protein</title><author>Poulin, Kathy L ; Clarkin, Ryan G ; Del Papa, Joshua ; Parks, Robin J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c330t-e224da878ec78455b091d3884555d1be4cae01e4ee9cb573f439b9da2643c1b03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>A549 Cells</topic><topic>Adenovirus E3 Proteins</topic><topic>Adenoviruses</topic><topic>Adenoviruses, Human - genetics</topic><topic>Analysis</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Cancer</topic><topic>Care and treatment</topic><topic>Cell death</topic><topic>Cell Line, Tumor</topic><topic>Control</topic><topic>Diagnosis</topic><topic>Gene expression</topic><topic>Genetic Vectors - genetics</topic><topic>Humans</topic><topic>Identification and classification</topic><topic>Infections</topic><topic>Metabolism</topic><topic>Mice</topic><topic>Oncolytic Virotherapy - methods</topic><topic>Oncolytic Viruses - genetics</topic><topic>Proteins</topic><topic>Risk factors</topic><topic>Viral Proteins - genetics</topic><topic>Viral Proteins - metabolism</topic><topic>Virus Replication - genetics</topic><topic>Viruses</topic><topic>Xenograft Model Antitumor Assays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Poulin, Kathy L</creatorcontrib><creatorcontrib>Clarkin, Ryan G</creatorcontrib><creatorcontrib>Del Papa, Joshua</creatorcontrib><creatorcontrib>Parks, Robin J</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Research Library (Corporate)</collection><collection>ProQuest Central (New)</collection><collection>ProQuest One Academic (New)</collection><collection>Publicly Available Content Database</collection><collection>ProQuest Health & Medical Research Collection</collection><collection>ProQuest One Academic Middle East (New)</collection><collection>ProQuest One Health & Nursing</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>International journal of molecular sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Poulin, Kathy L</au><au>Clarkin, Ryan G</au><au>Del Papa, Joshua</au><au>Parks, Robin J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Development and Characterization of an Oncolytic Human Adenovirus-Based Vector Co-Expressing the Adenovirus Death Protein and p14 Fusion-Associated Small Transmembrane Fusogenic Protein</atitle><jtitle>International journal of molecular sciences</jtitle><addtitle>Int J Mol Sci</addtitle><date>2024-11-20</date><risdate>2024</risdate><volume>25</volume><issue>22</issue><spage>12451</spage><pages>12451-</pages><issn>1422-0067</issn><issn>1661-6596</issn><eissn>1422-0067</eissn><abstract>Human adenovirus (HAdV)-based oncolytic vectors, which are designed to preferentially replicate in and kill cancer cells, have shown modest efficacy in human clinical trials in part due to poor viral distribution throughout the tumor mass. Previously, we showed that expression of the p14 fusion-associated small transmembrane (FAST) fusogenic protein could enhance oncolytic HAdV efficacy and reduce tumor growth rate in a human xenograft mouse model of cancer. We now explore whether co-expression of the adenovirus death protein (ADP) with p14 FAST protein could synergize to further enhance oncolytic vector efficacy. ADP is naturally encoded within the early region 3 (E3) of HAdV, a region which is frequently removed from HAdV-based vectors, and functions to enhance cell lysis and progeny release. We evaluated a variety of approaches to achieve optimal expression of the two proteins, the most efficient method being insertion of an expression cassette within the E3 deletion, consisting of the coding sequences for p14 FAST protein and ADP separated by a self-cleaving peptide derived from the porcine teschovirus-1 (P2A). However, the quantities of p14 FAST protein and ADP produced from this vector were reduced approximately 10-fold compared to a similar vector-expressing only p14 FAST protein and wildtype HAdV, respectively. Compared to our original oncolytic vector-expressing p14 FAST protein alone, reduced expression of p14 FAST protein and ADP from the P2A construct reduced cell-cell fusion, vector spread, and cell-killing activity in human A549 adenocarcinoma cells in culture. These studies show that a self-cleaving peptide can be used to express two different transgenes in an armed oncolytic HAdV vector, but also highlight the challenges in maintaining adequate transgene expression when modifying vector design.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>39596515</pmid><doi>10.3390/ijms252212451</doi><orcidid>https://orcid.org/0000-0003-2391-1010</orcidid><orcidid>https://orcid.org/0000-0002-8420-8903</orcidid><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1422-0067 |
ispartof | International journal of molecular sciences, 2024-11, Vol.25 (22), p.12451 |
issn | 1422-0067 1661-6596 1422-0067 |
language | eng |
recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_11594305 |
source | MDPI - Multidisciplinary Digital Publishing Institute; MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central |
subjects | A549 Cells Adenovirus E3 Proteins Adenoviruses Adenoviruses, Human - genetics Analysis Animals Apoptosis Cancer Care and treatment Cell death Cell Line, Tumor Control Diagnosis Gene expression Genetic Vectors - genetics Humans Identification and classification Infections Metabolism Mice Oncolytic Virotherapy - methods Oncolytic Viruses - genetics Proteins Risk factors Viral Proteins - genetics Viral Proteins - metabolism Virus Replication - genetics Viruses Xenograft Model Antitumor Assays |
title | Development and Characterization of an Oncolytic Human Adenovirus-Based Vector Co-Expressing the Adenovirus Death Protein and p14 Fusion-Associated Small Transmembrane Fusogenic Protein |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-21T18%3A00%3A07IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Development%20and%20Characterization%20of%20an%20Oncolytic%20Human%20Adenovirus-Based%20Vector%20Co-Expressing%20the%20Adenovirus%20Death%20Protein%20and%20p14%20Fusion-Associated%20Small%20Transmembrane%20Fusogenic%20Protein&rft.jtitle=International%20journal%20of%20molecular%20sciences&rft.au=Poulin,%20Kathy%20L&rft.date=2024-11-20&rft.volume=25&rft.issue=22&rft.spage=12451&rft.pages=12451-&rft.issn=1422-0067&rft.eissn=1422-0067&rft_id=info:doi/10.3390/ijms252212451&rft_dat=%3Cgale_pubme%3EA818337876%3C/gale_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=3133088733&rft_id=info:pmid/39596515&rft_galeid=A818337876&rfr_iscdi=true |