TASK DEFINITION: In this task, you're given a paragraph from the research paper and your task is to generate a suitable title for the research paper based on the given paper. Under 100 words is a good title length.
PROBLEM: The mucus-dwelling parasite Ostertagia ostertagi is one of the most important gastrointestinal nematodes in cattle. Our group has previously demonstrated the protective capacity of a vaccine against this parasite based on a native activation-associated secreted protein ASP1 (nASP) in combination with the saponin adjuvant QuilA. The aim of the current study was to analyse the effect of both antigen and adjuvant on the cellular and humoral vaccine-induced immune responses by comparing the native ASP to a recombinant version expressed in Pichia pastoris (pASP) and replacing QuilA by Al(OH) 3 . Immunization of cattle with the protective nASP+QuilA vaccine was associated with antigen-induced proliferation of natural killer (NK) cells combined with IFN- secretion and the induction of a mixed IgG1/IgG2 antibody response. ASP-specific activation and proliferation of NK cells was also observed in mice following the same vaccination regime. Replacing QuilA by Al(OH) 3 or nASP by pASP significantly decreased the capacity of the vaccines to trigger both NK cell activation and antibody responses and failed to induce protection against a challenge infection. Reduction of the structurally anchoring disulphide bonds of the nASP completely abolished its ability to induce NK cell activation and antibody responses, highlighting the importance of protein conformation for the immunostimulatory activity.

SOLUTION: Host protective ASP-based vaccine against the parasitic nematode Ostertagia ostertagi triggers NK cell activation and mixed IgG1-IgG2 response

PROBLEM: Protein chips have emerged as a promising approach for a wide variety of applications including the identification of protein-protein interactions, protein-phospholipid interactions, small molecule targets, and substrates of proteins kinases. They can also be used for clinical diagnostics and monitoring disease states. This article reviews current methods in the generation and applications of protein microarrays. Understanding complex cellular systems will require the identification and analysis of each of its components and determining how they function together and are regulated. A critical step in this process is to determine the biochemical activities of the proteins and how these activities themselves are controlled and modified by other proteins. Traditionally, the biochemical activities of proteins have been elucidated by studying single molecules, one experiment at a time. This process is not optimal, as it is slow and labor intensive. In contrast to this traditional approach, high-throughput scientific methods have been developed in the last decade to optimize the study of large numbers of molecules, including DNA, proteins and metabolites. DNA microarrays in particular have proved valuable in genomic research (Schena et al., 1995) . They have been used to study gene expression patterns, to locate transcription factor binding sites, and to detect sequence mutations and deletions on a grand scale. However, DNA microarrays tell us only about the genes themselves and provide little information regarding the functions of the proteins they encode. More recently high throughput approaches have been developed for the study of proteins, including profiling of proteins using mass spectrometry (Gavin et al.,

SOLUTION: Protein Microarray Technology Types of protein microarrays

PROBLEM: New possibilities for the design of coronavirus vaccines have been opened up with the elucidation of the structure of the receptorbinding domain (RBD) of severe acute respiratory syndrome (SARS) spike protein. The RBD of the SARS spike protein is responsible for virus attachment to its receptor, angiotensinconverting enzyme-2 (ACE2), on human cells. The RBD of the human epidemic strain differs from that of the animal virus by just two amino acids. Harrison and colleagues determined the complex of the interacting segments of these proteins, which consists of residues 19-615 of the peptidase domain of human ACE2 and residues 323-502 of the RBD, to 2.9-A resolution. The ACE2 peptidase domain comprises two lobes that close during substrate binding, and the spike RBD contacts the tip of one lobe when ACE2 is either open or closed. The RBD has a five-stranded, antiparallel -sheet core, and an extended-loop subdomain that lies along one edge of the core. A two-stranded -sheet in this loop forms a concave surface that cradles the N-terminal helix of ACE2, and ridges along either side of the loop interact with structural features of ACE2. This loop (residues 424-494) was named the receptor-binding motif (RBM) and makes the only contacts with ACE2, producing a 1,700 A 2 interface that is consistent with the high binding affinity of these proteins (K d ~10 -8 ). The detailed analysis of the contacts between these two proteins provides useful information for rational vaccine design. REFERENCE Li, F. et al. Structure of SARS coronavirus spike receptor-binding domain complexed with receptor.

SOLUTION:
STRUCTURE WATCH Spikes point the way