Virology Cell Lines
Membrane protein stable cell lines are widely used in many areas of biomedical research. Creative Biolabs can offer membrane protein stable cell lines to stablish in vitro models for High Throughput Screening.
Background of Virology
Virology is a subfield of microbiology that focuses on the study of the structure, taxonomy, infection, and reproduction of viruses and virus-like substances, as well as their physiology and immunity interactions with the host cell, and to understand the symptoms they cause and methods of treating them.
Mechanisms of Virus-Membrane Protein Interactions
Viruses can recognize receptors on the cell surface of specific tissues, normally, these receptors have a unique and invariant domain, which makes the virus infection often have a narrower range of host selection. After the initial binding, it is often accompanied by a secondary binding step between the virus and other components or proteins on the host cell membrane. The second interaction can enhance the adhesion of the virus or directly enter the cell through direct fusion or endocytosis. The fusion of viruses and cells often leads to dramatic changes in the fluidity and permeability of cell membranes and is likely to cause cell damage or death in the subsequent proliferation process.
Vertebral creatures recognize and resist viruses through their own immune systems. Immune T cells can recognize and attack infected host cells through HLA, immune checkpoints, or other immune-related proteins on the membrane, and proliferate virus-specific T cells in large numbers.
Applications and Pathology of Virology Cell Lines
A major motivation for studying viruses is that they cause many important infectious diseases, even includes Covid-19 and monkeypox. Research on the viruses that cause these severe diseases can help us better understand and cure them. Besides, the virus-receptor interactions clearly affect the species specificity of viral infection and may be an important determinant of viral tissue tropism in some cases. A better understanding of virus-receptor interactions will greatly advance the molecular basis of host specificity, vector capacity, and tissue tropism of specific viruses. In addition to the fundamental biological and clinical importance of viruses, they are also of practical interest, as the rational design of drugs that inhibit virus-receptor interactions at viral attachment or entry points provides a new approach to the treatment of viral diseases.
Published Data
| Paper Title | Structural and functional analysis of the roles of Influenza C virus membrane proteins in assembly and budding |
| Journal | Journal of Biological Chemistry |
| Published | 2022 |
| Abstract | Biologically, the assembly and budding process of the influenza C virus is divided into several steps, which are regulated by several key proteins, including matrix protein CM1, ion channel CM2 and hemagglutinin-esterase-fusion (HEF) glycoprotein. These three proteins are also all membrane proteins encoded by the influenza C virus. Influenza C virus membrane proteins have been explored in depth in previous studies, but it remains unclear how the functions of CM1 and HEF are coupled together. Likewise, the relevance of CM1 to virus-like particles and vesicle membranes remains to be explored. In the present experiment, the researchers investigated whether the hexagonal arrangement of HEFs is directly related to the viral budding process. Using confocal microscopy and super-resolution microscopy to visualize plasmid-expressed influenza C virus membrane proteins, the researchers identified HEF clusters that were insensitive to cytochalasin and cholesterol extraction. Amino acids in the open HEF conformation and the HEF trimer structure were then exchanged to determine their roles in viral replication and virus-like particle (VLP) generation. The results of this experiment can be compared with those of similar viral membrane proteins, especially those published for influenza A virus membrane proteins, to reveal differences or similarities in the budding of influenza viruses. |
| Result |
In conclusion, research on the influenza C virus shows that the budding and multiplication process of the influenza C virus is similar to but different from that of the influenza A virus. Most surprisingly, CM1 was not detected in the nuclei of transfected cells, suggesting that nuclear export of the viral genome occurs by a different mechanism than that established for influenza A and B. In the absence of other viral proteins, CM1 is translocated to the plasma membrane, whereas M1 is retained in the Golgi apparatus. CM1, like M1, can release membrane vesicles into the supernatant of transfected cells if it is localized on the plasma membrane, suggesting that it can bend membranes and form vesicles. Like M2, CM2 can also form tubular membranes, possibly using an amphipathic helix adjacent to the transmembrane region. Surface amino acid substitution experiments in the HEF trimer conformation suggest that a completely different mechanism may exist in the budding process of the influenza C virus, that is, the external shell is formed through lateral interactions between the ectodomains of the glycoprotein HEF. In some other virus families, such as flaviviruses, budding is also primarily driven by interactions between membrane glycoproteins. However, they form a flat, symmetrical icosahedral lattice that drives viral morphogenesis primarily through interactions between transmembrane helices. In contrast, influenza C viruses are pleomorphic, and the sole spike protein HEF does not lie flat on the membrane but instead forms long surface protrusions. Flu A does not display a regular network of its glycoproteins HA and NA, but lateral interactions may involve smaller neuraminidase NA clusters observed at the ends of filamentous virions or VLPs. In conclusion, we propose that lateral interactions between HEF trimer ectodomains are the driving force for viral budding, although CM2 and CM1 also play important roles in this process.
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