Exploring host-pathogen interactions through genome wide protein microarray analysis.
27996 - ?
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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.
AuthorsScietti, L; Sampieri, K; Pinzuti, I; Bartolini, E; Benucci, B; Liguori, A; Haag, AF; Lo Surdo, P; Pansegrau, W; Nardi-Dei, V; Santini, L; Arora, S; Leber, X; Rindi, S; Savino, S; Costantino, P; Maione, D; Merola, M; Speziale, P; Bottomley, MJ; Bagnoli, F; Masignani, V; Pizza, M; Scharenberg, M; Schlaeppi, J-M; Nissum, M; Liberatori, S
- College Publications