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.

Background: Influenza is a zoonotic disease that infects millions of people each year resulting in hundreds of thousands of deaths, and in turn devastating pandemics. Influenza is caused by influenza viruses, including influenza A virus (IAV). There are many subtypes of IAV but only a few seem to be able to adapt to humans and to cause disease. In 2013, an H7N9 IAV subtype emerged in China that does not cause clinical symptoms in its chicken host but leads to severe infections when transmitted into humans. Since 2013, there have been six epidemic waves of H7N9 with 1567 laboratory-confirmed human infections and 615 deaths. Pathogenicity of IAV is complex, but a crucial feature contributing to virulence is the activation of the hemagglutinin (HA) fusion protein by host proteases that triggers membrane fusion and leads to subsequent virus propagation. : 293T, VERO, and MDCK cells were used to conduct Western blot analysis, immunofluorescence assays, and pseudoparticle and live virus infections, and to evaluate H7N9 HA cleavage-activation. Results/Conclusions: We show that human matriptase/ST 14 is able to cleave H7N9 HA. Cleavage of H7N9 HA expressed in cell culture results in fusogenic HA and syncytia formation. In infection studies with viral pseudoparticles carrying matriptase/ ST 14-activated H7N9 HA, we observed a high infectivity of cells. Finally, human matriptase/ST 14 also activated H7N9 live virus which resulted in high infectivity. Our data demonstrate that human matriptase/ST 14 is a likely candidate protease to promote H7N9 infections in humans.
Human matriptase/ST 14 proteolytically cleaves H7N9 hemagglutinin and facilitates the activation of influenza A/Shanghai/2/2013 virus in cell culture

Synthetic decapeptides (N ¼ 206) covering the entire sequence of mouse liver fumarylacetoacetate hydrolase (FAH) were used to analyze the specificities of the autoantibodies (autoAb) elicited towards this enzyme in mice infected with mouse hepatitis virus (MHV). These autoAb bound mainly to N-and C-terminal FAH peptides, the most reactive sequences being 1e50 and 390e420, respectively. Surprisingly, although FAH sequence 1e50 shares a high degree of homology with various MHV proteins, the C-terminal portion does not. Moreover, whereas the autoAb reacted with homologous peptides surrounding residues 70, 160 and 360, non-similar sequences around residues 130, 210, 240, 250, and 300 were also recognized, indicating that autoAb were not restricted to epitopes with sequence homologies. There was also a lack of correlation between the amount of anti-MHV or anti-FAH antibodies produced and the reactivity towards the peptides. Moreover, the spectrum of peptides recognized by the autoAb of a given mouse did not change significantly with time, which suggests that the MHV-elicited autoimmune response does not induce an epitope recognition spreading. Finally, anti-FAH Ab produced after immunization with rat liver FAH recognized essentially the same mouse FAH regions than autoAb from MHV-infected mice. Results indicated that the induction of the autoAb is not only related to molecular or structural mimicry, but rather supports the Danger model, in which any aggression, in this case the MHV infection, is susceptible to trigger the production of autoAb.
The peptide specificities of the autoantibodies elicited by mouse hepatitis virus A59

Background/Aims: The clinical pattern of cryptosporidial diarrhea suggests an enterotoxic mechanism. No evidence for this mechanism has been reported thus far. This study aimed.to look for enterotoxic effect elaborated by Cryptosporidium. Methods: The effects on human intestinal transport of stool supematant of diarrheal calves infected with Cryptosporidium parvum were examined. Aliquots of centrifuged and filtered stools were added to the mucosal or serosal side of human jejunum obtained from patients undergoing surgery and mounted in Ussing chambers. Electrical parameters were recorded. Stool supernatants of uninfected calves served as a control. Results: The mucosal addition of 2.5 mg protein of fecal supernatant from diarrheal calves induced a prompt and significant increase in short circuit current with no effects on tissue conductance. The serosal addition of this material and the addition of control supernatant to either side did not induce modifications of electrical parameters. The enterotoxic effect was dose-dependent and saturable. It was reversible by withdrawing the supernatant from the incubation medium. The electrical effect was chloride-and calcium-dependent and was sensitive to heating. Conclusions: An enterotoxic activity is present in the stools of Cryptosporidiurr~infected calves. This activity may be responsible for secretory diarrhea in humans.

Enterotoxic Effect of Stool Supernatant of Cryptosporidium- Infected Calves on Human Jejunum