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.

Input: Consider Input: We tested the role of the "spring-loaded" conformational change in the fusion mechanism of the influenza hemagglutinin (HA) by assessing the effects of 10 point mutants in the region of high coiled-coil propensity, HA2 54-81. The mutants included proline substitutions at HA2 55, 71, and 80, as well as a double proline substitution at residues 55 and 71. Mutants were expressed in COS or 293T cells and assayed for cell surface expression and structural features as well as for their ability to change conformation and induce fusion at low pH. We found the following: Specific mutations affected the precise carbohydrate structure and folding of the HA trimer. All of the mutants, however, formed trimers that could be expressed at the cell surface in a form that could be proteolytically cleaved from the precursor, HA0, to the fusion-permissive form, HA1-S-S-HA2. All mutants reacted with an antibody against the major antigenic site and bound red blood cells. Seven out of ten mutants displayed a wild-type (wt) or moderately elevated pH dependence for the conformational change. V55P displayed a substantial reduction ( 60-80%) in the initial rate of lipid mixing. The other single mutants displayed efficient fusion with the same pH dependence as wt-HA. The double proline mutant V55P/ S71P displayed no fusion activity despite being well expressed at the cell surface as a proteolytically cleaved trimer that could bind red blood cells and change conformation at low pH. The impairment in fusion for both V55P and V55P/S71P was at the level of outer leaflet lipid mixing. We interpret our results in support of the hypothesis that the spring-loaded conformational change is required for fusion. An alternate model is discussed.

Output: Specific Single or Double Proline Substitutions in the "Spring-loaded" Coiled-Coil Region of the Influenza Hemagglutinin Impair or Abolish Membrane Fusion Activity

Input: Consider Input: . The role of interferon in spontaneous cell-mediated cytotoxicity in pigs. Vet. Microbiol., I i : 69 -77. Specific release of StCr and the production of interferon (IFN) increased in parallel in a spontaneous cell-mediated cytotoxicity (SCMC) assay in which uninfected PK-15 cells or PK-15 cells persistently infected with transmissible gastroenteritis virus (PK-15-TGE cells) were used as targets, and peripheral blood lymphocytes (PBL) from a young adult pig were used as effector cells. Higher levels of both specific S~Cr release and IFN were obtained in the assays containing PK-15-TGE cells. Co-cultivation of PBL from newborn piglets with PK-15-TGE cells yielded similar levels of IFN to those produced by co-cultivation of adult PBL and PK-15-TGE cells, but lower levels of IFN were produced by co-cultivation with uninfected PK-15 cells. Pretreatment of adult PBL with IFN augmented their SCMC effector activity for both PK-15 and PK-15-TGE cells in the S~Cr release assay. Pretreatment of the PK-15-TGE target cells with IFN did not affect their release of S*Cr in the SCMC reaction, while IFN pretreatment of PK-15 targets protected them against SCMC. In a single cell cytotoxicity assay the effects of IFN pretreatment on the effector adult PBL and on the PK-15 and PK-15-TGE target cells were confirmed, and SCMC incompetent PBL from neonatal piglets were rendered cytotoxic by pretreatment with IFN. PBL from newborn piglets bound to either target cell with the same frequency as PBL from SCMC competent adult pigs, and IFN pretreatment of either effector or target cells had no effect on target-binding frequency.

Output: THE ROLE OF INTERFERON IN SPONTANEOUS CELL-MEDIATED CYTOTOXICITY IN PIGS

Input: Consider Input: Mis-secreted glycoproteins (LGI1, reelin) are emerging causes of epilepsy. LMAN2L belongs to a glycoprotein secretion chaperone family. One recessive LMAN2L missense mutation predicted to impair the chaperone's interaction with glycoproteins was reported in a family with intellectual disability (ID) and remitting epilepsy. We describe four members of a family with autosomal dominant inheritance of a similar phenotype. We show that they segregate a NM_001142292.1:c.1073delT mutation that eliminates LMAN2L's endoplasmic reticulum retention signal and mislocalizes the protein from that compartment to the plasma membrane. LMAN2L mislocalization, like impaired glycoprotein interaction, disturbs brain development, including generation of developmentally restricted epilepsy.
Output: Dominant LMAN2L mutation causes intellectual disability with remitting epilepsy