A Finite Element Analysis of the Biomechanical Effects of a Novel Pedicle Screw W-Type Rod Fixation for Lumbar Spondylolysis

Kheryl Lucie^*
*Correspondence: Kheryl Lucie, Department of Medicine & Advanced Technology, University of Helsinki, Helsinki, Finland, Email:

Keywords

Nucleocapsid • Genome • Envelope • Replicase

Introduction

One of the salutary repercussions of SARS-CoV-2 is that it has led to an increased focus on the importance of public health measures such as handwashing, social distancing, and mask-wearing. These measures have been shown to be effective in reducing the spread of the virus, and could have broader implications for preventing the spread of other infectious diseases in the future. In addition, the emergence of new strains of the virus has led to increased surveillance and monitoring of viral mutations, which could have implications for the development of new vaccines and antiviral drugs. By understanding how the virus evolves and adapts to new conditions, scientists can better predict which strains are most likely to be prevalent in the future, and develop more effective treatments to combat them [1]. Furthermore, the search for effective antiviral drugs has led to promising developments in the field of drug discovery. Several antiviral drugs have shown promise in treating COVID-19, including remdesivir, which has been granted emergency use authorization by the FDA. Other drugs, such as hydroxychloroquine and ivermectin, have shown mixed results in clinical trials, but have nevertheless contributed to the growing body of knowledge about how to treat the disease. One of the most promising areas of research in the search for antiviral drugs is the development of monoclonal antibodies, which are synthetic antibodies designed to target specific viral proteins. Several monoclonal antibody treatments have been authorized for emergency use in the US, including Regeneron's casirivimab and imdevimab, which have been shown to reduce hospitalization rates and improve outcomes in patients with mild to moderate COVID-19 [2]. Another area of research that shows promise is the development of oral antiviral drugs that can be taken at home. Several companies, including Pfizer and Merck, are currently developing oral antiviral drugs that could be used to treat COVID-19 in the early stages of the disease. These drugs could be particularly useful in settings where hospitalization is not feasible or practical, such as in developing countries with limited healthcare infrastructure [3].

Literature Review

Despite these promising developments, there are still many challenges in the search for effective antiviral drugs for COVID-19. One of the biggest challenges is the rapidly evolving nature of the virus, which makes it difficult to develop drugs that can target all strains of the virus. In addition, there are logistical challenges in distributing and administering antiviral drugs on a large scale, particularly in low-income countries with limited healthcare infrastructure [4]. Nevertheless, the ongoing research into SARS-CoV-2 and its strains, as well as the development of new antiviral drugs, offers hope for the future. By continuing to invest in scientific research and public health measures, we can work towards a world where the impact of infectious diseases like COVID-19 is minimized, and where we are better prepared to respond to future outbreaks and pandemics [5].

Discussion

Because of the instability of the single-stranded RNA structure and the difficulty in correcting errors during viral replication, RNA viruses tend to mutate more easily. SARS-CoV-2 has undergone multiple mutations as COVID-19 spreads in the human population. Virus mutation is a random process that can occur at any stage and location in the replication process. However, some research has found that mutations in the S protein increase pathogenicity and infectivity. Because of its greater impact on social prevalence, the S protein mutation is considered a variant of concern (VOC). The S protein, as a structural protein of SARS-CoV-2 primarily mediates the virus's binding to the angiotensin-converting enzyme 2 (ACE2) receptor. A large number of SARSCoV- 2 variants have been discovered to date, with five significant variants receiving extensive attention: Alpha, Beta, Gamma, Delta, and Omicron. Because the mutants' transmissibility and pathogenicity are enhanced to varying degrees, therapeutic strategies for the mutants have been extensively researched [6].

In this review, we will provide a brief overview of the five variants mentioned above, as well as a summary of current potential therapeutic strategies and molecular targets for these variants. H69/V70 is defined as a deletion of histidine 69 and valine 70 at the NTD site, which can result in significant immune evasion after infection in immunocompromised patients and increase the virus's infectiousness. Interactions between viral mutation sites, as seen in SARS-CoV-2, have the potential to confer transmissibility and virulence to the virus. Some studies have found a superimposed effect between H69/V70 and D614G or N439K mutations, indicating that H69/V70 and D614G mutant strains exhibit faster cell-cell fusion kinetics than wild-type virus strains.

However, because the in vitro experiments did not include a systemic immune barrier, a large number of studies are required to confirm the immune escape caused by H69/V70 deletion. The N501Y mutation is characterized by a tyrosine (Y) substitution of aspartic acid (N) at position 501, with the mutation site primarily located in the S gene's receptor binding motif (RBM) region. As previously stated, S region mutations can increase the affinity of the virus receptor to varying degrees. The virus's binding strength to ACE2 is significantly increased in the N501Y strain, and there is evidence that the affinity of the B.1.1.7 strain for ACE2 is increased by 110%, while the affinity for neutralizing antibodies is only slightly increased [7].

Conclusion

Furthermore, RBD is the primary target of plasma antibody neutralisation activity, and studies have shown that the E484K mutation can reduce the efficacy of antibody therapy and lead to immune escape. Furthermore, K417N has been shown to induce a conformational change in the S protein, making the virus difficult to recognise by antibodies and increasing the virus's infectivity. As previously stated mutations in the S gene predispose the variant to immune evasion and increased affinity for the receptor. As a result, E484K, N501Y, and K417N play an important role in the toxicity of the Beta variants. Deep mutational scans have revealed that E484K increases the ACE2 receptor's binding affinity.

Acknowledgement

None.

Conflict of Interest

None.

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