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.

The respiratory syncytial virus (RSV) fusion (F) glycoprotein is a major target of neutralizing antibodies arising from natural infection, and antibodies that specifically bind to the prefusion conformation of RSV F generally demonstrate the greatest neutralization potency. Prefusion-stabilized RSV F variants have been engineered as vaccine antigens, but crystal structures of these variants have revealed conformational differences in a key antigenic site located at the apex of the trimer, referred to as antigenic site . Currently, it is unclear if flexibility in this region is an inherent property of prefusion RSV F or if it is related to inadequate stabilization of site in the engineered variants. Therefore, we set out to investigate the conformational flexibility of antigenic site , as well as the ability of the human immune system to recognize alternative conformations of this site, by determining crystal structures of prefusion RSV F bound to neutralizing human-derived antibodies AM22 and RSD5. Both antibodies bound with high affinity and were specific for the prefusion conformation of RSV F. Crystal structures of the complexes revealed that the antibodies recognized distinct conformations of antigenic site , each diverging at a conserved proline residue located in the middle of an -helix. These data suggest that antigenic site exists as an ensemble of conformations, with individual antibodies recognizing discrete states. Collectively, these results have implications for the refolding of pneumovirus and paramyxovirus fusion proteins and should inform development of prefusion-stabilized RSV F vaccine candidates. Respiratory syncytial virus (RSV) is a pervasive pathogen that causes severe lower respiratory tract infections, leading to~100,000 deaths globally each year and hundreds of millions of dollars in healthcare costs. However, despite its prevalence, there is no vaccine for RSV and the only available therapy is limited to high-risk infants, leaving the vast majority of people with no effective means of prevention or treatment. The RSV fusion (F) protein is a major target of neutralizing antibodies, including extremely potent antibodies that PLOS Pathogens | https://doi.recognize prefusion-specific epitopes. In this study, we determined the crystal structures of two neutralizing human antibodies bound to prefusion RSV F. Our results reveal that each antibody recognizes a different conformation of a neutralization-sensitive epitope, suggesting that this region is inherently flexible and may be important for RSV F function. These results should guide future vaccine-design efforts and help elucidate the mechanisms of RSV F triggering and fusion. Conformational flexibility of antigenic site PLOS Pathogens | https://doi.
Alternative conformations of a major antigenic site on RSV F

Background-The potential risks associated with "toilet plume" aerosols produced by flush toilets is a subject of continuing study. This review examines the evidence regarding toilet plume bioaerosol generation and infectious disease transmission. Methods-The peer-reviewed scientific literature was searched to identify articles related to aerosol production during toilet flushing, as well as epidemiologic studies examining the potential role of toilets in infectious disease outbreaks. Results-The studies demonstrate that potentially infectious aerosols may be produced in substantial quantities during flushing. Aerosolization can continue through multiple flushes to expose subsequent toilet users. Some of the aerosols desiccate to become droplet nuclei and remain adrift in the air currents. However, no studies have yet clearly demonstrated or refuted toilet plume-related disease transmission, and the significance of the risk remains largely uncharacterized. Conclusion-Research suggests that toilet plume could play a contributory role in the transmission of infectious diseases. Additional research in multiple areas is warranted to assess the risks posed by toilet plume, especially within health care facilities. An association between inhalable bioaerosols produced from disturbed sewage and the transmission of infectious disease has been proposed for over 100 years. However, little study has been devoted to characterizing the potential risks posed by the "toilet plume" Gerba et al 10 seeded a siphonic gravity-flow toilet with Escherichia coli and sequentially placed 3 arrays of settle plates on the floor around the toilet, with each set exposed for 2 Johnson et al.
Lifting the lid on toilet plume aerosol: A literature review with suggestions for future research

Arenaviruses and hantaviruses cause severe human disease. Little is known regarding host proteins required for their propagation. We identified human proteins that interact with the glycoproteins (GPs) of a prototypic arenavirus and hantavirus and show that the lectin endoplasmic reticulum (ER)-Golgi intermediate compartment 53 kDa protein (ERGIC-53), a cargo receptor required for glycoprotein trafficking within the early exocytic pathway, associates with arenavirus, hantavirus, coronavirus, orthomyxovirus, and filovirus GPs. ERGIC-53 binds to arenavirus GPs through a lectin-independent mechanism, traffics to arenavirus budding sites, and is incorporated into virions. ERGIC-53 is required for arenavirus, coronavirus, and filovirus propagation; in its absence, GP-containing virus particles form but are noninfectious, due in part to their inability to attach to host cells. Thus, we have identified a class of pathogen-derived ERGIC-53 ligands, a lectin-independent basis for their association with ERGIC-53, and a role for ERGIC-53 in the propagation of several highly pathogenic RNA virus families.
The Intracellular Cargo Receptor ERGIC-53 Is Required for the Production of Infectious Arenavirus, Coronavirus, and Filovirus Particles