Together, urine peptidomics and targeted plasma profiling revealed a urine biomarker panel of 17-urine peptides and a plasma biomarker panel of six plasma proteins as SJIA flare signatures. Shown in Fig. 5 , our integrated analyses suggest that the differential abundance of urine peptides in SJIA urine may be an outcome of both the pathophysiological changes initiated by IL-18 and RANTES and P/L-Selectinmediated inflammatory responses and the function of leukocyte-derived TIMP1/MMP9; the latter would influence protein catabolism in SJIA. The inflammatory cytokines may also directly affect levels of expression of substrate proteins and influence levels of expression of peptide derivatives of these proteins. Evaluation of urine peptide profiles in future prospective studies will test the robustness and diagnostic/prognostic values of these urine peptide biomarkers and may provide new insights into SJIA pathogenesis. Segmented Helical Structure of the Neck Region of the Glycan-Binding Receptor DC-SIGNR Carbohydrate-recognition domains (CRDs) in the glycan-binding receptors DC-SIGN (dendritic-cell-specific intercellular adhesion molecule 1-grabbing nonintegrin; CD209) and DC-SIGNR (DC-SIGN-related receptor, also known as L-SIGN and variously designated CD209L and CD299) are projected from the membrane surface by extended neck domains containing multiple repeats of a largely conserved 23-amino-acid sequence motif. Crystals of a fragment of the neck domain of DC-SIGNR containing multiple repeats in which each molecule extends through multiple unit cells, such that the observed crystallographic asymmetric unit represents one repeat averaged over six repeats of the protein, have been obtained. The repeats are largely α-helical. Based on the structure and arrangement of the repeats in the crystal, the neck region can be described as a series of four-helix bundles connected by short, non-helical linkers. Combining the structure of the isolated neck domain with a previously determined overlapping structure of the distal end of the neck region with the CRDs attached provides a model of the almost-complete extracellular portion of the receptor. The results are consistent with previous characterization of the extended structure for the isolated neck region and the extracellular domain. The organization of the neck suggests how CRDs may be disposed differently in DC-SIGN compared with DC-SIGNR and in variant forms of DC-SIGNR assembled from polypeptides with different numbers of repeats in the neck domain.  Translation Elongation Factor 1A Facilitates the Assembly of the Tombusvirus Replicase and Stimulates Minus-Strand Synthesis Replication of plus-strand RNA viruses depends on host factors that are recruited into viral replicase complexes. Previous studies showed that eukaryotic translation elongation factor (eEF1A) is one of the resident host proteins in the highly purified tombusvirus replicase complex. Using a random library of eEF1A mutants, we identified one mutant that decreased and three mutants that increased Tomato bushy stunt virus (TBSV) replication in a yeast model host. Additional in vitro assays with whole cell extracts prepared from yeast strains expressing the eEF1A mutants demonstrated several functions for eEF1A in TBSV replication: facilitating the recruitment of the viral RNA template into the replicase complex; the assembly of the viral replicase complex; and enhancement of the minus-strand synthesis by promoting the initiation step. These roles for eEF1A are separate from its canonical role in host and viral protein translation, emphasizing critical functions for this abundant cellular protein during TBSV replication. Genome-wide screens for host factors affecting RNA virus infections have led to the identification of several hundreds host proteins in recent years [1, 2, 3, 4, 5, 6, 7] . These works demonstrated complex interactions between the host and plus-stranded (+)RNA viruses, the largest group among viruses. (+)RNA viruses contain relatively small genomes and greatly depend on the resources of the infected hosts in many steps during the infection process. These viruses recruit numerous host proteins to facilitate their replication and spread [8, 9, 10] . Many host RNA-binding proteins have been implicated in replication of (+)RNA viruses, including ribosomal proteins, translation factors and RNA-modifying enzymes [8, 9, 10, 11, 12, 13, 14] . In spite of the extensive effort, the actual function of host factors in (+)RNA virus replication is known only for a small number of host factors [8, 10, 15, 16, 17] .