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Aggregation is mediated by type IV pili and can be modulated by accessory pilus proteins, such as PilX, and posttranslational modifications of the major pilus subunit PilE. The mechanisms underlying the regulation of aggregation remain poorly characterized. Polynucleotide phosphorylase (PNPase) is a 3\u2032\u20135\u2032 exonuclease that is involved in RNA turnover and the regulation of small RNAs. In this study, we biochemically confirm that NMC0710 is the\n            <jats:named-content content-type=\"genus-species\">N. meningitidis<\/jats:named-content>\n            PNPase, and we characterize its role in\n            <jats:named-content content-type=\"genus-species\">N. meningitidis<\/jats:named-content>\n            pathogenesis. We show that deletion of the gene encoding PNPase leads to hyperaggregation and increased adhesion to epithelial cells. The aggregation induced was found to be dependent on pili and to be mediated by excessive pilus bundling. PNPase expression was induced following bacterial attachment to human cells. Deletion of PNPase led to global transcriptional changes and the differential regulation of 469 genes. We also demonstrate that PNPase is required for full virulence in an\n            <jats:italic>in vivo<\/jats:italic>\n            model of\n            <jats:named-content content-type=\"genus-species\">N. meningitidis<\/jats:named-content>\n            infection. The present study shows that PNPase negatively affects aggregation, adhesion, and virulence in\n            <jats:named-content content-type=\"genus-species\">N. meningitidis<\/jats:named-content>\n            .\n          <\/jats:p>","DOI":"10.1128\/iai.01463-15","type":"journal-article","created":{"date-parts":[[2016,3,1]],"date-time":"2016-03-01T03:34:22Z","timestamp":1456803262000},"page":"1501-1513","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":24,"title":["Neisseria meningitidis Polynucleotide Phosphorylase Affects Aggregation, Adhesion, and Virulence"],"prefix":"10.1128","volume":"84","author":[{"given":"Jakob","family":"Engman","sequence":"first","affiliation":[{"name":"Department of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, Stockholm, 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