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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.
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Coronaviruses most often infect the respiratory or intestinal tract. Transmissible gastroenteritis virus (TGEV), a group 1 coronavirus, infects the porcine small intestine. Piglets up to the age of 3 weeks die from diarrhea caused by the viral gastroenteritis unless they are protected by antibodies. In addition to the cellular receptor, porcine aminopeptidase N, the TGEV spike protein binds to sialic acid residues. We have shown that the sialic acid binding activity mediates the binding of TGEV to a mucin-like glycoprotein present in porcine brush border membranes. This was shown by performing a virus overlay binding assay with proteins obtained from brush border membranes by lectin precipitation. Because of the reactivity with specific lectins we assume that the recognized glycoprotein has the characteristics of a mucin.
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Identification of Sugar Residues Involved in the Binding of TGEV to Porcine Brush Border Membranes


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Graphical Abstract Highlights d Binding to all influenza A subtypes neutralizing seasonal and pandemic strains d Utilizes a rare VH (VH6-1) and carries a low level of somatic mutations d Highly conserved epitope encompassing fusion peptide and hydrophobic groove d Superior therapeutic window compared to oseltamivir in animals Correspondence zhuq@medimmune.com (Q.Z.), john.skehel@crick.ac.uk (J.J.S.) In Brief Identification of a human monoclonal antibody that reacts effectively with all influenza A hemagglutinin subtypes paves the way for developing immunotherapy for people infected with the flu virus. Accession Numbers 5JW5 5JW4 5JW3 KX398429 KX398468 SUMMARY Influenza virus remains a threat because of its ability to evade vaccine-induced immune responses due to antigenic drift. Here, we describe the isolation, evolution, and structure of a broad-spectrum human monoclonal antibody (mAb), MEDI8852, effectively reacting with all influenza A hemagglutinin (HA) subtypes. MEDI8852 uses the heavy-chain VH6-1 gene and has higher potency and breadth when compared to other anti-stem antibodies. MEDI8852 is effective in mice and ferrets with a therapeutic window superior to that of oseltamivir. Crystallographic analysis of Fab alone or in complex with H5 or H7 HA proteins reveals that MEDI8852 binds through a coordinated movement of CDRs to a highly conserved epitope encompassing a hydrophobic groove in the fusion domain and a large portion of the fusion peptide, distinguishing it from other structurally characterized cross-reactive antibodies. The unprecedented breadth and potency of neutralization by MEDI8852 support its development as immunotherapy for influenza virus-infected humans.
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Structure and Function Analysis of an Antibody Recognizing All Influenza A Subtypes Article Structure and Function Analysis of an Antibody Recognizing All Influenza A Subtypes


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Two fragments, S66 and S55, of the S glycoprotein of the newly identified canine coronavirus type I (CCoV type I), were expressed in a procariotic system. The purified recombinant proteins of 350 and 366 amino acids in length, respectively, were employed to develop an enzyme-linked immunosorbent assay (ELISA) for the detection of CCoV type I antibodies in dog sera. Four canine sera-positive for CCoV type II, four sera-positive for CCoV type I and 10 negative control sera were examined. Only the sera-positive for CCoV type I strongly reacted with both the proteins, whereas the sera-positive for CCoV type II showed low reactivity in the ELISA test. As CCoV type I seems to be not cultivable in cell cultures, the recombinant fragments of the S protein represent a unique method to study, preliminarily, the immunological and the pathogenetic characteristics of this new virus.
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Cloning and expression of two fragments of the S gene of canine coronavirus type I