<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Cheng M</submitter><funding>NIDCD NIH HHS</funding><pagination>1457-1470</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8742275</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>32(23-24)</volume><pubmed_abstract>Adeno-associated virus (AAV) is classified as a nonenveloped DNA virus. However, several years ago, we discovered that in media of packaging cells producing recombinant AAV vectors, AAV capsids can associate with the interior and surface of extracellular vesicles (EVs), sometimes referred to as exosomes. Since then, we and others have demonstrated that exosome-enveloped AAV, exo-AAV, can enhance transduction &lt;i>in vivo&lt;/i> as well as evade neutralizing antibodies. While promising, these data were generated with differential centrifugation to pellet the exo-AAV. This method results in a heterogeneous mixture of exo-AAV, coprecipitating proteins, as well as free AAV capsids. To define the properties of exo-AAV more accurately, in this study, we used a density gradient method to purify exo-AA</pubmed_abstract><journal>Human gene therapy</journal><pubmed_title>Neutralizing Antibody Evasion and Transduction with Purified Extracellular Vesicle-Enveloped Adeno-Associated Virus Vectors.</pubmed_title><pmcid>PMC8742275</pmcid><funding_grant_id>R01 DC017117</funding_grant_id><pubmed_authors>Nammour J</pubmed_authors><pubmed_authors>Dietz L</pubmed_authors><pubmed_authors>Ng C</pubmed_authors><pubmed_authors>Eichler F</pubmed_authors><pubmed_authors>Cheng M</pubmed_authors><pubmed_authors>Maguire CA</pubmed_authors><pubmed_authors>Gong Y</pubmed_authors><pubmed_authors>Grimm D</pubmed_authors></additional><is_claimable>false</is_claimable><name>Neutralizing Antibody Evasion and Transduction with Purified Extracellular Vesicle-Enveloped Adeno-Associated Virus Vectors.</name><description>Adeno-associated virus (AAV) is classified as a nonenveloped DNA virus. However, several years ago, we discovered that in media of packaging cells producing recombinant AAV vectors, AAV capsids can associate with the interior and surface of extracellular vesicles (EVs), sometimes referred to as exosomes. Since then, we and others have demonstrated that exosome-enveloped AAV, exo-AAV, can enhance transduction &lt;i>in vivo&lt;/i> as well as evade neutralizing antibodies. While promising, these data were generated with differential centrifugation to pellet the exo-AAV. This method results in a heterogeneous mixture of exo-AAV, coprecipitating proteins, as well as free AAV capsids. To define the properties of exo-AAV more accurately, in this study, we used a density gradient method to purify exo-AA</description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Dec</publication><modification>2025-04-03T21:30:18.036Z</modification><creation>2025-04-03T21:30:18.036Z</creation></dates><accession>S-EPMC8742275</accession><cross_references><pubmed>34445894</pubmed><doi>10.1089/hum.2021.122</doi></cross_references></HashMap>