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.

[EX Q]: Severe fever with thrombocytopenia syndrome (SFTS) is an emerging infectious 24 disease localized to China, Japan, and Korea that is characterized by severe hemorrhage and a 25 high fatality rate. Currently, no specific vaccine or treatment has been approved for this 26 disease. To develop a therapeutic agent for SFTS, we isolated antibodies from a phage-27 displayed antibody library that was constructed from a patient who recovered from SFTS 28 virus (SFTSV) infection. One antibody, designated as Ab10, was reactive to the Gn envelope 29 glycoprotein of SFTSV and protected host cells and A129 mice from infection in both in 30 vitro and in vivo experiments. Notably, Ab10 protected 80% of mice, even when injected 5 31 days after inoculation with a lethal dose of SFTSV. Using cross-linker assisted mass 32 spectrometry and alanine scanning, we located the non-linear epitope of Ab10 on the Gn 33 glycoprotein domain II and an unstructured stem region, suggesting that Ab10 may inhibit a 34 conformational alteration that is critical for cell membrane fusion between the virus and host 35 cell. Ab10 reacted to recombinant Gn glycoprotein in Gangwon/Korea/2012, HB28, and SD4 36 strains. Additionally, based on its epitope, we predict that Ab10 binds the Gn glycoprotein in 37 247 of 272 reported SFTSV isolates previously reported. Together, these data suggest that 38 Ab10 has potential to be developed into a therapeutic agent that could protect against more 39 than 90% of reported SFTSV isolates. 40 41
[EX A]: An anti-Gn glycoprotein antibody from a convalescent patient potently 2 inhibits the infection of severe fever with thrombocytopenia syndrome virus

[EX Q]: Several polypeptide products of MHV-A59 ORF 1 a were characterized in MHV-A59 infected DBT cells, using antisera directed against fusion proteins encoded in the first 6.5 kb of ORFla. These included the previously identified N-terminal ORF 1 a product, ~28, as well as 290-, 240-, and 50-kDa polypeptides. P28 was always detected as a discrete band without larger precursors, suggesting rapid cleavage of p28 immediately after its synthesis. Once p28 was cleaved there was little degradation of the protein over a 2-hr period. The intracellular cleavage of p28 was not inhibited by the protease inhibitor leupeptin, in contrast to results obtained during in vitro translation of genome RNA (Denison and Perlman, 1986). These data suggest that different protease activities may be responsible for the cleavage of p28 in vitro and in Go. The 290-kDa protein was an intermediate cleavage product derived from a precursor of greater than 400 kDa. The 290-kDa product was subsequently cleaved into secondary products of 50 and 240 kDa. The intracellular cleavage of the 290-kDa polypeptide was inhibited by leupeptin at concentrations which did not inhibit the early cleavage of p28 or the cleavage of the 290-kDa product from its larger polyprotein precursor. In the presence of zinc chloride, a product of >320 kDa was detected, which appears to incorporate p28 at its amino terminus. This suggests that at least two protease activities may be necessary for processing of ORFl a proteins, one of which cleaves p28 and is sensitive to zinc chloride but resistant to leupeptin, and the other which cleaves the 290-kDa precursor and is sensitive to both inhibitors. Both the 290-and 240-kDa proteins should contain sequences predicted to encode two papain-like prOtesS? activities. 0 1992 Academic PVE.S. Inc.
[EX A]: Intracellular Processing of the N-Terminal ORF la Proteins of the Coronavirus MHV-A59 Requires Multiple Proteolytic Events

[EX Q]: The complement system plays a crucial role in host defense against pathogen infections and in the recognition and removal of damaged or altered selfcomponents. Complement system activation can be initiated by three different pathways-classical, alternative, and lectin pathways-resulting in a proteolytic cascade, which culminates in multiple biological processes including opsonization and phagocytosis of intruders, inflammation, cell lysis, and removal of immune complexes and apoptotic cells. Furthermore, it also functions as a link between the innate and adaptive immune responses. The lectin pathway (LP) activation is mediated by serine proteases, termed mannan-binding lectin (MBL)associated serine proteases (MASPs), which are associated with the pattern recognition molecules (PRMs) that recognize carbohydrates or acetylated compounds on surfaces of pathogens or apoptotic cells. These result in the proteolysis of complement C2 and C4 generating C3 convertase (C4b2a), which carries forward the activation cascade of complements, culminating in the elimination of foreign molecules. This chapter presents an overview of the complement system focusing on the characterization of MASPs and its genes, as well as its functions in the immune response.
[EX A]:
8 Serine Proteases in the Lectin Pathway of the Complement System