which approaches one uniformly on .H2 as n increases for any a.o. p, since H(Q) 2 2. The same procedure is used for &',, but the sequence is-+ KL.LMhk,). *-+ p(h(j,,j,))p(h(k,,k,)) * *. so that the 2" integers mapped by h" are always drawn from the same distribution (Q, or Q,). Using this encoding on the rows of the array in Fig. I, sending representations of 2" runs of zeros and 2" runs of ones from each row, and using the appropriate marker-moving algorithm gives an a.o. sequence of universal codes for SZZ~, A, and JZ'.

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Staphylococcus aureus, sequence type (ST) 398, is an emerging pathogen and the leading cause of livestock-associated methicillin-resistant S. aureus infections in Europe and North America. This strain is characterized by high promiscuity in terms of host-species and also lacks several traditional S. aureus virulence factors. This does not, however, explain the apparent ease with which it crosses species-barriers. Recently, TIR-domain containing proteins (Tcps) which inhibit the innate immune response were identified in some Gram-negative bacteria. Here we report the presence of two proteins, S. aureus TIR-like Protein 1 (SaTlp1) and S. aureus TIR-like Protein 2 (SaTlp2), expressed by ST398 which contain domain of unknown function 1863 (DUF1863), similar to the Toll/IL-1 receptor (TIR) domain. In contrast to the Tcps in Gram-negative bacteria, our data suggest that SaTlp1 and SaTlp2 increase activation of the transcription factor NF-κB as well as downstream pro-inflammatory cytokines and immune effectors. To assess the role of both proteins as potential virulence factors knock-out mutants were created. These showed a slightly enhanced survival rate in a murine infectious model compared to the wild-type strain at one dose. Our data suggest that both proteins may act as factors contributing to the enhanced ability of ST398 to cross species-barriers.

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