Exploring host-pathogen interactions through genome wide protein microarray analysis

During bacterial pathogenesis extensive contacts between the human and the bacterial extracellular proteomes take place. The identification of novel host-pathogen interactions by standard methods using a case-by-case approach is laborious and time consuming. To overcome this limitation, we took adva...

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Published inScientific reports Vol. 6; no. 1; p. 27996
Main Authors Scietti, Luigi, Sampieri, Katia, Pinzuti, Irene, Bartolini, Erika, Benucci, Barbara, Liguori, Alessia, Haag, Andreas F, Lo Surdo, Paola, Pansegrau, Werner, Nardi-Dei, Vincenzo, Santini, Laura, Arora, Seguinde, Leber, Xavier, Rindi, Simonetta, Savino, Silvana, Costantino, Paolo, Maione, Domenico, Merola, Marcello, Speziale, Pietro, Bottomley, Matthew J, Bagnoli, Fabio, Masignani, Vega, Pizza, Mariagrazia, Scharenberg, Meike, Schlaeppi, Jean-Marc, Nissum, Mikkel, Liberatori, Sabrina
Format Journal Article
LanguageEnglish
Published England Nature Publishing Group 15.06.2016
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Summary:During bacterial pathogenesis extensive contacts between the human and the bacterial extracellular proteomes take place. The identification of novel host-pathogen interactions by standard methods using a case-by-case approach is laborious and time consuming. To overcome this limitation, we took advantage of large libraries of human and bacterial recombinant proteins. We applied a large-scale protein microarray-based screening on two important human pathogens using two different approaches: (I) 75 human extracellular proteins were tested on 159 spotted Staphylococcus aureus recombinant proteins and (II) Neisseria meningitidis adhesin (NadA), an important vaccine component against serogroup B meningococcus, was screened against ≈2300 spotted human recombinant proteins. The approach presented here allowed the identification of the interaction between the S. aureus immune evasion protein FLIPr (formyl-peptide receptor like-1 inhibitory protein) and the human complement component C1q, key players of the offense-defense fighting; and of the interaction between meningococcal NadA and human LOX-1 (low-density oxidized lipoprotein receptor), an endothelial receptor. The novel interactions between bacterial and human extracellular proteins here presented might provide a better understanding of the molecular events underlying S. aureus and N. meningitidis pathogenesis.
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ISSN:2045-2322
2045-2322
DOI:10.1038/srep27996