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Who Was Ty Jochmans? Get all the details on the man whose online obituary has intrigued netizens.
Ty Jochmans was an American hunter and social worker. He was a notable member of Wounded Veterans Of Oklahoma (WVO), a nonprofit organization dedicated to helping war veterans.
The organization helps retired war veterans to show their respect financially, personally, and in many other ways.
Known as one of the core members of the organization, he was portrayed as a star within the group, and his death brought many Oklahoma resents up to date.
Who Was Ty Jochmans?
Ty Jochmans was a professional hunter and adventure gue. He had devoted his life to hunting, community service and his family.
Therefore, he was known as a perfect man devoted to his work and family.
In fact, he founded the WVO Outdoors site and was one of the well-known WVO Outdoor Gues who took veterans on hunting trips.
Known for his unwavering love of adventures such as travel and hunting, he was one of the most popular men in the organization.
Ase from his services for WVO, he also worked at Tk Whitetails and Exotics in the same space.
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Ty Jochmans Obituary: Know His Death Cause
Ty Jochman’s official obituary is still being documented, while the exact cause of death has also not been disclosed.
The official announcement of his death was shared by WVO on their official page without mentioning his cause of death.
The Jochmann family is still mourning the loss of a very young son.
Ase from his girlfriend and employers, the official obituary will be posted very soon for the brave heart of Oklahoma’s funeral.
His Age And Wikipedia Explored
Ty Jochman’s exact age is not disclosed, although his birthday falls on September 22 every year.
Sadly, he passed away just one day after his big day, leaving his family and friends to mourn.
He is survived by his young son Denver and his family. Meanwhile, not much is currently available about the Jochmann family.
He also loved his girlfriend Arielle-Ann, with whom he raised his 4-year-old son.
Arielle is a fitness guru and bodybuilder. Likewise, according to his social media posts, particularly on Facebook and Instagram, his son Denver also got involved after his hunts.
He was certainly a brave father who taught his son the basics of hunting ethics.
Now that he’s gone, his social media is filled with messages of rest in peace.
Obituary: Who is Ty Jochman? Death Cause, Age, Wife, Family, Lifestyle, Net worth, Biography, Birth
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Obituary: Who Was Ty Jochmans? Death Cause Explored – TVW Wiki
Ty Jochman’s official obituary is still in the process of documentation while the exact cause of his death has also not been shared.
Source: wiki.tvw.net
Date Published: 11/10/2021
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Ty Jochmans Death | Obituary |… – The Arts of Entertainment
Ty Jochmans Death | Obituary | Dead | Died | Funeral Plans – It is with great sadness to announce the passing of Ty Jochmans. We are made to know about…
Source: ne-np.facebook.com
Date Published: 1/26/2021
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r/DeathObituaries – TY Jochmans Death – Obituary News: Y …
Anyone know what happened to him? They are not saying a cause of death and I’m wondering if it was suice.
Source: www.reddit.com
Date Published: 3/16/2022
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Ty Jochmans Oklahoma Obituary – The Arts of Entertainment
Ty Jochmans cause of death has not been made public. We pray that God grants those mourning this death the strength and the courage to carry on.
Source: theartsofentertainment.com
Date Published: 6/29/2022
View: 8711
Obituary News Y Jochmans of Oklahoma has died . Click link to read full story. DeathObituaries
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Newly Emerged Antiviral Strategies for SARS-CoV-2 From Deciphering Viral Protein Structural Function to the Development of Vaccines, Antibodies, and Small Molecules
This review updates the structure and function of SARS-CoV-2 proteins according to the latest literature reports, including S, M, N, E and NSP1-NSP16. Here we mainly focus on the newly deciphered structure and function of SARS-CoV-2 proteins as they were predicted or referenced according to the sequence and structure of SARS-CoV-1. In addition, we summarize the newly developed anti-SARS-CoV-2 treatment strategies including antibodies, vaccines and small molecules.
The COVID-19 pandemic caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a highly contagious disease [1]. The outbreak of COVID-19 led to a global pandemic and resulted in huge casualties with a high number of deaths (total 6,075,512 deaths, March 20, 2022) and infections (total 469,833,166 confirmed cases, March 20, 2022) worldwide [ 2 ]. COVID-19 disease causes more severe conditions for the immunocompromised population and accelerates the progression of other diseases [3]. SARS-CoV-2 virus is a single-stranded, enveloped, positive-sense RNA virus belonging to β-coronavirus [4]. The proteins encoded by the genome of SARS-CoV-2 consist of structural (SPs) and nonstructural proteins (NSPs) as well as accessory proteins [5, 6]. SPs mainly include spike (S), membrane (M), envelope (E) and nucleocapsid (N) proteins [7]. NSPs contain open reading frames (ORFs), including ORF1a and ORF1b regions. There are 16 NSPs in the ORF1a and ORF1b regions [5]. A schematic of the genome-encoded proteins of SARS-CoV-2 is summarized in one figure (Figure 1).
Nucleocapsid (N): The N protein, which encapsulates the viral genome, plays a fundamental function in viral RNA transcription, replication, and assembly [27]. Several groups reported that inhibition of RNA-induced N-protein phase separation by bioactive molecules can disrupt the SARS-CoV-2 replication cycle [28, 31]. N protein can inhibit the phosphorylation of the signal transducer and activator of transcription 1 (STAT1) and STAT2, resulting in inactivation of the host interferon (IFN) signaling pathway. Consequently, the viruses can evade the host’s IFN-mediated antiviral response [32]. An in vitro study showed that N protein can induce phosphorylation of nuclear factor (NF)-ĸB p65 and modulate production of pro-inflammatory cytokines and M1 polarization of macrophages. The results mentioned were further confirmed by treatment with denatured N-protein and N-protein antibodies. In a mouse model, N-protein-mediated activation of NF-κB signaling induced acute lung injury [33]. Therefore, N protein is also an attractive target for research into treatment of COVID-19 [27, 34].
Envelope (E): The E protein not only plays an important role as an ion transporter in viral morphogenesis, but also serves as a virulence factor. The envelope protein of SARS-CoV-2 demonstrates the function of E-mediated virulence [22]. A study showed an interaction between the viral E protein and the tight junction protein of human lung epithelium PALS1 (Lin-seven 1 associated protein) or MPP5 (membrane-associated palmitoylated protein 5). In the study, the researchers provided structure-based evidence for the interaction between the E and PALS1 proteins [23]. This structural discovery further explained the underlying mechanism of biological phenomena. It supports evidence that high levels of E protein were expressed in SARS-CoV-2 infected lung tissues [24]. Another well-designed study showed that the E protein virulence factor can modulate the immune response by repressing and inducing the inflammasome Nod-like receptor protein 3 (NLRP3) at different stages of infection. The authors emphasized the importance of targeting the SARS-Cov-2 E protein for the development of vaccines or therapeutic strategies [25,26]. By collaborating with analysis of virus structure and infectivity, we can better understand the underlying mechanism of COVID-19 infection and find a precise target for treatment.
Membrane (M): The M protein belongs to the structural proteins. It encompasses the viral envelope and contributes to viral morphogenesis [7, 16]. The similarity of the genomic sequences encoding the M proteins between SARS-CoV-1 and SARS-CoV-2 is significantly high [17, 19]. The information about the M protein of SARS-CoV-1 thus provides valuable information for further investigation of the newly emerged SARS-CoV-2. Recently, scientists applied bioinformatic tools and found detailed structural information of the M protein in SARS-CoV-2. Although there are some amino acid differences between SARS-CoV-2 and SARS-CoV-1, they share a similar protein structural property. For example, both M proteins show hydrophobic features in the transmembrane domains and hydrophilic features in the N-terminus and C-terminus. The properties of hydrophilicity and hydrophobicity are both critical to vaccine development. In the same study, the authors also found potential B-cell epitopes that could be associated with recognition of antibodies from the host’s immune response. These epitopes have the potential to be used for further vaccine development or treatment targets [20]. Another group using in silico analyzes found a three-helix transmembrane domain of M protein in SARS-CoV-2, forming a sugar transporter-like structure with respect to semiSWEET. The structure of semiSWEET indicates that M protein may play multifunctional roles such as sugar transport and metabolism. This interesting finding stimulates further investigation of M protein function [21].
The decoding of structural information and functional properties of S protein plays an important role in understanding the interactions and underlying mechanisms between host and viral infection. Recently, researchers discovered that SARS-CoV-2 uses the structural function of the S protein to weaken or evade host immune surveillance. For example, it has been shown that there is an association between the high affinity of SARS-CoV-2 variants of concern (VOCs) and the mechanical stability of the S/ACE2 complex, which induces immune escape and spread of delta and omicron variants . The mutations of N501Y (alpha, beta, gamma and omicron), E484Q (beta, gamma and omicron) and omicron E484A contribute to the increased binding affinity between RBD and ACE2 [11,12]. Furthermore, the mechanical stability of the SARS-CoV-2 RBD/S protein appears to protect the virus in the upper airway region under mechanical forces compared to SARS-CoV-1 [13]. Furthermore, since the viral fusion protein is coated with a greater thickness of N-glycan, glycosylation is essential for viral virulence. Mutations of N165A and N234A cause deletion of glycans, resulting in weakened binding affinity. Remarkably, it has been the center of debate in this field about the structural changes (close to open) mediated by N-glycan located on the S-protein [14]. Therefore, treatments that control S protein conformation could be a target for vaccine application [15].
Spike (S): The SARS-CoV-2 S protein is widely studied due to its crucial role in virus entry into host cells. The S protein comprises two functional subunits S1 and S2. The S1 subunit plays an important role in viral recognition and binding of the human angiotensin converting enzyme 2 (hACE2) receptor. The S2 subunit is responsible for membrane fusion between host and virus membranes. These two steps are necessary for SARS-CoV-2 to enter host cells. Thus, S protein facilitates viral invasion into host cells [8]. SARS-CoV-2 enters host cells via two different fusion pathways [9], either by direct fusion with the cell membrane to release the virtual genome RNA or by endocytosis through membrane fusion of the viral membrane with a host cell membrane. The process of virus entry, infection and replication is illustrated by a schematic diagram (Figure 2). The virus receptor binding domain (RBD) contains several antigenic epitopes. These antigenic epitopes, also known as antigenic determinants, are the binding sites of host antibodies. The antigenic epitope plays an important role in activating the immune response of the host’s CD4 and CD8 T cells [10]. Therefore, the S protein, the RBD domain, and antigenic epitopes pave the way for the development of vaccines and therapeutic strategies. However, the virus also adapts to increase its ability to invade and infect. The effectiveness of vaccines and therapies is subject to the most common mutation.
1.3. SARS-CoV-2 nonstructural proteins
NSP1: The NSP1 of SARS-CoV-2 has been reported to play a pivotal role in repressing translation of host mRNA. Meanwhile, NSP1 facilitates translation of viral mRNA. In other words, NSP1 can disable host mRNA translation and shift the process to viral mRNA translation in infected cells. NSP1 shifts host ribosome function in a two-pronged mechanism. First, the C-terminal domain of viral NSP1 can bind directly to the 40S ribosomal subunit to block binding of host mRNAs, resulting in repression of host mRNA translation. Second, NSP1 can overcome this inhibition by interacting with a 5′ untranslated region (5′ UTR) of SARS-CoV-2 mRNA with the N-terminal domain of NSP1. Thus, viral mRNA can be translated by the host ribosome [35]. Therefore, viral NSP1 plays an essential role in converting the infected cell from a site for host mRNA translation into a site for viral mRNA translation. This finding sparks interest in exploring potential therapeutic options by targeting NSP1.
2+ exchange in endoplasmic reticulum (ER) and involved in mitochondrial biogenesis [NSP2: NSP2 has been found to be associated with Ca exchange in endoplasmic reticulum (ER) and involved in mitochondrial biogenesis [36]. A recent study found that SARS-CoV-2 NSP2 contains a conserved zinc binding site associated with binding RNA. The structural analysis also revealed that the protein surface of NSP2 evolves rapidly, which could possibly be related to the interaction of NSP2 and the host [37]. A number of studies and analyzes also uncovered that NSP2 may contribute to virus-host interaction such as: B. the interactions with endosomes, ribosomal RNAs and translation modulators [ 37 ]. Although more research is needed to further evaluate the function of NSP2, current studies shed light on the potential of using NSP2 as one of the therapeutic targets.
NSP3: NSP3, also known as papain-like protease, is responsible for cleaving the viral polypeptides NSP1-4 [37]. Recently, a new function of SARS-CoV-2 NSP3 was reported. The study showed that NSP3 can also cleave interferon regulatory transcription factor 3 (IRF3) directly, resulting in an attenuated type I IFN response [38]. As a result, SARS-CoV-2 infection causes the disruption of the host’s antiviral response. Another study also showed the interaction between the NSP3/papain-like protease (PLpro) and antiviral host proteins such as IFN-associated proteins [39]. An in silico study revealed the molecular mechanism of the interaction between NSP3 and the C-terminal domain of the viral N-phosphoprotein. The major residues involved in the binding site have been analyzed using the molecular docking method [40]. The above studies offer inspiring insights into the potential of using NSP3 as a target for therapeutic development, including vaccines and NSP3 inhibitors.
NSP4: Aside from its crucial role in viral replication, a recent study has shown that NSP4 plays a role in ER homeostasis. In this study, the highly enriched NSP4 and NSP2 of SARS-CoV-2 were detected in mitochondria-associated ER membranes (MAM). The authors also found that there are common NSP4 interactors for different viruses (SARS-CoV-1, SARS-CoV-2 and hCoV-OC43), such as and unique NSP4 interactors for SARS-CoV-2, such as the monoubiquitin ribosomal fusion protein (RPS27A), a Golgi/ER-resident zinc receptor and necroptosis (SLC39A7), and the ER-resident Hsp70 chaperone BiP (HSPA5) [36]. ER homeostasis is essential for host cell survival. Disruption of ER homeostasis caused by viral infection could lead to ER stress and cell dysfunction, which is essential for virus replication and maturation [41].
NSP5: NSP5, also known as 3C-like protease (3CLpro), plays an important role in influencing the host’s immune response. Similar to NSP3, NSP5 can also cleave IRF3 directly to block the Type I IFN response. Meanwhile, NSP5 can cleave the pyrine domain of the NLR family containing 12 (NLRP12) and TAK1-binding proteins (TAB) to increase the production of inflammatory cytokines and affect the downstream signaling pathway [38]. A remarkable discovery identified the differential mechanism of NSP5 in the host immune signaling pathway. NSP5 directly cleaves the amino acids of retinoic acid-inducible gene I (RIG-I) and consequently disables its ability to activate mitochondrial antiviral signaling (MAVS). In addition, NSP5 also plays the function of promoting the degradation of MAVS. The study also showed that NSP5 can interact with RIG-I or MAVS to suppress antiviral immune responses such as B. the inhibition of IFN expression [42]. In a separate study, scientists found that NSP5 caused significantly increased expression of cytokines such as interleukin (IL)-1β, IL-6, IL-2 and tumor necrosis factor alpha (TNF-α) in a non-small cell lung cancer cell line, Calu -3 and a monocyte cell line THP1. The molecular mechanism study further showed that NSP5 increased the protein levels of MAVS and led to the activation of the nucleic factor (NF)-κB signaling pathway by regulating SUMOylation of MAVS. NSP5-mediated activation of the NF-κB pathway can be attenuated by knockdown of MAVS or inhibition of SUMOylation [43]. In conclusion, NSP5 is an attractive target due to its association with host immune response and cytokine storm.
+ Transport accessory protein 1) and trigger the inflammasome to induce pyroptosis, resulting in severe inflammatory cell death. The NSP6-L37F point mutation decreased binding affinity with ATP6AP1, resulting in less damage to virus-infected cells. In addition, the epidemiological analysis showed that the NSP6-L37F mutation was associated with asymptomatic COVID-19 infection in human patients. In short, NSP6 can be further studied as one of the important therapeutic targets, especially from the perspective of inflammation [44, NSP6: A study found that SARS-CoV-2 NSP6 impeded autophagy function in lung epithelial cells. Autophagy is the protective mechanism for host cells to suppress inflammasome activation. NSP6 can directly bind to ATP6AP1 (ATPase Htransporting accessory protein 1) and trigger the inflammasome to induce pyroptosis, resulting in severe inflammatory cell death. The NSP6-L37F point mutation decreased binding affinity with ATP6AP1, resulting in less damage to virus-infected cells. In addition, the epidemiological analysis showed that the NSP6-L37F mutation was associated with asymptomatic COVID-19 infection in human patients. In short, NSP6 can be further explored as one of the important therapeutic targets, especially from the perspective of inflammation [18, 45].
NSP7, NSP8 and NSP12: Most interestingly, scientists have successfully obtained the cryo-EM structure of a core polymerase complex comprising NSP7, NSP8 and NSP12 of SARS-CoV-2. This complex is known as the RNA-dependent RNA polymerase (RdRp) complex, which provides structure-based evidence for the interaction between these three proteins. In this polymerase complex, NSP7 and NSP8 serve as cofactors while NSP12 serves as the catalytic subunit. The study also found that there is high identity of the sequence structure of NSP7 and NSP8 compared to the bat coronavirus counterpart RaTG13; However, there are four differences in NSP12 between SARS-CoV-2 and the bat coronavirus RaTG13. Meanwhile, the study showed that the thermostability of the polymerase subunit was lower in SARS-CoV-2 than in bat coronavirus. This observed divergence in thermostability of viral polymerases between humans and bats could be explained from the perspective of virus evolution. Viruses adapt to human body temperature by reducing their thermostability for viral replication due to body temperature differences between humans and bats [46].
NSP9: The biochemical study of SARS-CoV-2 has shown that nucleoside monophosphate (NMP)ylation of NSP9 is essential for viral replication. The N-terminus of NMPylation of NSP9 was catalyzed and mediated by the Nidovirus RdRp-associated nucleotidyltransferase (NiRAN) domain of NSP12. Mutation studies were performed to identify the critical residues in NiRAN-mediated NSP9 NMPylation and viral replication. The results indicated that the N3826 residue of NSP9 plays an important role in the interaction between NSP9 and NSP12 as well as in viral replication, giving insight into the possibility of a drug targeting site [47].
NSP10-NSP14 Complex: NSP14 is guanine N7 methyltransferase (ExoN). Nsp10 coupled with NSP14 forms the NSP10-NSP14 complex. A well-designed study clarified that the NSP10-NSP14 complex functions as a function of RNase. RNase activity was enhanced by the presence of the RNA polymerase complex (a complex of NSP12-NSP7 and NSP8). NSP8 played an important role in increasing the activity of the NSP10-NSP14 complex. In addition, the study also showed that the NSP10–NSP14 complex contributed to repairing RNA replication, with the exception of the classic proofreading function. When RNA replication has stalled due to unpredictable reasons, the NSP10–14 complex can mediate the repair process with RNase activity to maintain extension continuity [48]. Another study found that NSP14 has antagonistic properties to IFN [49]. Therefore, these discoveries also provide a rationale for targeting these NSPs.
NSP10-NSP16 Complex: NSP16 is an RNA methyltransferase. The NSP10–NSP16 complex plays a crucial role in the methylation of viral RNA at the 2′-O position of ribose. This methylation resulted in a change in the viral RNA cap into a structure that mimics host cell mRNAs. Using this mechanism, SARS-CoV-2 could evade the host’s innate immune system [50]. Structural analysis demonstrated the attractiveness of attacking this protein complex as an antiviral strategy by developing an inhibitor to block nucleotide binding sites [51].
NSP11: Remarkably, NSP11 is a very short peptide for SARS-CoV-2, consisting of only 13 amino acids. A molecular dynamics simulation study identified that NSP11 functions as an intrinsically disordered protein. The conformational change in NSP11 from disorder to order depends on the membrane environment. This finding indicates that NSP11 may contribute to the interaction between the virus and the host cell membrane. Due to its important role at the cellular level, it should be further studied [52].
NSP12: NSP12 is also known as RdRp. In addition to forming a complex with NSP7 and NSP8, NSP12 has been shown to be associated with the receptor-interacting serine/threonine protein kinase 1 (RIPK1) signaling pathway. Cytokine storm is the leading cause of death in COVID-19 patients. RIPK1, a known inflammatory mediator, contributes to inflammation and cell death. RIPK1 activation has been identified in human patients with COVID-19 infection. Inhibition of RIPK1 by inhibitors can decrease viral load in cultured lung organoids from human COVID-19 patients. In addition, administration of a therapeutic dose of RIPK1 inhibitors reduced mortality in virus-infected ACE2 transgenic mice, as well as reduced viral loads. They further discovered that NSP12 is responsible for RIPK1 activation, since amino acid variations of NSP12 resulted in different levels of activation of RIPK1 signaling pathway [53]. These results illustrate the important association between NSP12 and the RIPK1 inflammatory signaling pathway. Therefore, targeting NSP12 is a treatment approach.
NSP13: NSP13 is a helicase protein. It is responsible for the replication of the virus genome. The cryo-EM structure showed that NSP13 forms a unique complex together with NSP7, NSP8 and NSP12. A zinc-binding domain is located at the N-terminus of NSP13 while the helicase domain is located at the C-terminus. Together they confer powerful enzymatic functions such as B. Unwinding of RNA/DNA helicase (5′-3′), RNA 5′-triphosphatase, NTPase and dNTPase. Given the multifunctional and essential roles of this complex, NSP13 is highly conserved between SARS-CoV-1 and SARS-CoV-2, with only a single amino acid variation at position 570 (Ile for SARS-CoV-1 and Val for SARS -CoV-2) . NSP13 was found to possess significant interferon antagonizing property [49]. This makes NSP13 one of the most promising drug targets for virus therapeutic strategies [ 54 55 ].
NSP15: The endoribonuclease of the coronavirus is encoded by NSP15. Previous studies on SARS-CoV-1 discovered that NSP15-encoded endoribonuclease can cleave the virus’ 5′-polyuridine RNA and facilitate virus escape from host macrophage detection [56,57]. The SARS-CoV-2 NSP15 also showed strong interferon-antagonizing properties [49].
In conclusion, both the SPs and NSPs of SARS-CoV-2 play essential roles in viral infection, COVID-19 pathogenesis, and host immune interaction. Unraveling the structure-function properties of the virus and the underlying mechanisms associated with infection is crucial for the development of treatments.
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