3d structure of hantavirus

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  • Jan 31, 2020

RCSB PDB - 5LK0: Structure of hantavirus envelope glycoprotein Gc ...
RCSB PDB – 5LK0: Structure of hantavirus envelope glycoprotein Gc …

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1Institute of Fundamental Medicine and Biology, Federal University of Kazan, Kazan, Russia

1Institute of Fundamental Medicine and Biology, Federal University of Kazan, Kazan, Russia

1Institute of Fundamental Medicine and Biology, University of federal Kazan, Kazan, Russia

2Nevada Center for Biomedical Research, Reno, NV, USA

3Department of Pathology and Nevada State Laboratory of Public Health, University of Nevada School of Medicine, Reno, NV, USA

1Institute of Fundamental Medicine and Biology, University of federal Kazan, Kazan, Russia

Hantaviruses is a member of the family Bunyaviridae reared naturally in small mammal populations, mostly rodents. Most of this virus can easily infect humans through contact with aerosol or dust produced by animal waste products contaminated. Depending on the particular hantavirus involved, infection in humans can result in either dengue fever with renal syndrome or in hantavirus cardiopulmonary syndrome. In recent years, clinical cases of hantavirus caused the disease has increased. Hantavirus understanding of genome structure and function of key viral protein is very important to study therapeutic agents. This paper provides a brief overview of the current knowledge on the structure and properties of hantavirus nucleoprotein and glycoproteins.

Hantaviruses comprises Hantavirus genus in the family Bunyaviridae (). Humans are infected by one virus inhaling contaminated aerosols or having contact with urine or feces of infected animals (). In humans well hantaviruses cause hemorrhagic fever with renal syndrome (HFRS) or hantavirus cardiopulmonary syndrome (HCP). Generally, each different hantavirus is maintained in nature in certain populations of small mammals (rodents or insectivores) host species. Murinae associated hantaviruses cause HFRS, while Sigmodontinae usually associated hantaviruses cause HCP. Most Arvicolinae-borne hantaviruses (Prospect Hill virus and Tula virus being the most prominent) apparently non-pathogenic to humans (;). In accordance with the geographical distribution of natural hosts a particular virus, HFRS is mainly diagnosed in Europe and Asia, with murine-borne virus Hantaan (HTNV), Dobrava-Belgrade virus (DOBV), and viral Seoul, as well as arvicoline-borne virus Puumala (PUUV), airport as the major causative agent. HCP is endemic in the United States and is caused by a variety of Sigmodontinae-borne New World Hantaviruses, Andes virus (ANDV) and Sin Nombre virus (SNV) became the most prominent source of human infection. The death rate varies from 0.3 to 10% for HFRS and between 30 and 40% for HCP (;;). HFRS clinical symptoms including fever, renal dysfunction, hemorrhagic manifestations and shock. HCP is characterized by fever, myalgia, headache, and gastrointestinal symptoms, followed by non-cardiogenic pulmonary edema and shock. Summary geographical distribution and host affiliate hantaviruses most prominent and diseases that cause given in the Table.

Representatives hantaviruses and their rodent hosts.

Hantavirus virions have a spherical shape with sizes varying between 80 and 120 nm. Hantavirus genome consists of three segments of single-stranded RNA negative sense. Based on their size, these three segments are named small (S), medium (M) and large (L). L segment encodes the viral polymerase, whereas the M and S segment encodes a precursor (GPC) for two viral surface glycoproteins (G1 and G2, or alternatively called Gn and Gc), and the nucleocapsid (N) protein, respectively. Each virion generally contain the same molar amount of genomic RNA, with a single molecule of the virus RNA-dependent RNA polymerase (RdRp) that is attached to each segment of the viral RNA. All viral RNA segments are coated with N protein molecules to form ribonucleoproteins (RNPs;). It is flanked by an envelope composed of a lipid bilayer, with G1 and G2 surface glycoproteins embedded into it ().

Hantavirus virion attachment to host cells through cellular receptors followed by endocytosis. RNPs released into the cytoplasm of the following late endosome pH-mediated membrane fusion. Transcription and translation take place either at the site of the release of RNPs or in endoplasmic reticulum-Golgi intermediate compartment (ERGIC). In the latter case, RNPs are transported to ERGIC. Viral polymerase, RdRp, having transcriptase, an endonuclease replicase and function; thus, it brings out both viral transcription (Figure) and replication (Figure). To initiate transcription, RdRp cleave cellular mRNA primary form is limited. More recently, cellular endonuclease has also been suggested to participate in the primary formation is limited by splitting the cellular mRNA cap-structure is protected from degradation by the N protein specifically bound to the virus (). This primer is limited initiate transcription of the viral mRNA. S segments derived mRNA serves as a template for the protein N, and for some specific hantaviruses also produce non-structural protein NSs (Figure). M segment derived mRNA produce GPC on ribosomes bound to the ER membrane. G1 and G2 glycoprotein complex transported from the ER to the Golgi or plasma membrane where assembly takes place (Figure). Old World hantaviruses gathered in the Golgi while New World hantaviruses gathered at the plasma membrane (;;) (Figure). After assembly, the newly formed envelope containing spike-like projections (;;) is formed by a tetramer of the viral surface glycoprotein, which seems to play an important role in both viral assembly and cell entry (;;). newly assembled virions released by exocytosis.

Hantavirus transcription, replication and translation.
(A) Hantavirus transcription. Transcription occurs through a mechanism primed and realign. Cellular mRNA cleaved by one hantavirus RNA-dependent RNA polymerase (RdRp) or cellular endonucleases in a process called cap snatching, thus forming a capped primer (m7GpppNn). It is this capped primer which initiates transcription by aligning guanidine to 3 ‘cytosine of vRNA. After synthesis of several nucleotides, the nascent RNA slip back and realigns. elongation end then takes place, producing additional copies of the viral mRNA. (B) Replication hantavirus RNA. Replication occurs in the cytoplasm of infected cells, using a prime and realign mechanism. RdRp attached to the 3 ‘end of the vRNA lumped guanidine triphosphate (PPPG) cytosine residues with the first of the viral RNA and synthesizing the first three nucleotides of the new Crna strand. Nascent RNA slip back and realigns after successive addition of bases. Then, the final extension lasted so long Crna full production. In turn, the positive Crna anti-genomic strand serves as a template to generate a large number of new strands vRNA. (C) Hantavirus transcription and translation. Negative sense viral RNA serves as a template for viral RdRp, which initiate transcription of the cap-snatching mechanism and produce viral mRNA. viral mRNAs are translated to produce the N protein, glycoprotein precursor (which is cleaved to form glycoproteins G1 and G2), and RdRp from small (S), medium (M) and large (L) segment-derived mRNA, respectively.

Hantavirus lifecycle. Virion binds to the cell surface membrane receptors and enter the cell by endocytosis. Once inside the cell, RNPs released from the endosome end through pH-mediated membrane fusion. Virion-supplied RdRp driving early mRNA transcription takes place in the cytoplasm. Viral genomic (minus sense) RNA serves as a template for the generation of mRNA are used for protein synthesis. When sufficient amounts of viral proteins are produced, RdRp switch to synthetic replication of the full length anti-genomic (plus sense) RNA, which in turn serves as a template for producing a large number of viral RNA molecules full of flavor new reduced length. Newly synthesized vRNA becomes encapsidated by the N protein to form ribonucleoprotein and transported to the perinuclear membrane system, from where they will be transported to the Golgi to the initiation of virion formation. Way out takes place at the plasma membrane.

Hantavirus surface glycoproteins G1 and G2 by code segments M and is expressed as a precursor polyprotein, GPC, which is cleaved by a cellular protease during translocation into the ER produce mature G1 and G2 glycoprotein (Figure) (;). cryo-electron microscopy and cryo-electron tomography studies have shown that the G1 and G2 proteins form a square-shaped spikes protruding from the surface of the virus membrane, with each spike complex made of four subunits four G1 and G2 (;). It has been proven that heterodimers G1 / G2 glycoprotein can interact withsurface of certain cellular proteins, β3-integrin, facilitate the entry of hantaviruses cause cellular HCP ().

Both G1 and G2 glycoprotein that is built in the same way, each containing a large globular domain, a hydrophobic transmembrane sequence and cytoplasmic tail of small C-terminal. Because there is no connecting hantavirus matrix proteins nucleoproteins and envelope protein, it is suggested that there is a direct interaction between the N protein and the cytoplasmic tail of G1 and G2. Nuclear magnetic resonance spectroscopy has shown that part of the tail G1 (residues 543-599) has a zinc finger ββα double fold consists of a highly conserved motif which has a high similarity between ANDV and Prospect Hill virus (PHV) (,). It has been suggested that these zinc fingers play a role in virus assembly ().

bunyavirus glycoprotein maturation takes place in the Golgi complex (). During maturation, G1 and G2 glycoprotein is N-glycosylation. Three glycosylation sites located in the G1 and G2 glycoprotein only one. Both G1 and G2 glycoprotein sensitive to endoglycosidases H and F. It has been reported that G1 and G2 are targeting to Golgi conformations depending on the interaction between these two glycoproteins (;). In addition, it appears that the G1 glycoprotein plays an important role in facilitating trade between the two glycoproteins Golgi. For example, when the G1 glycoprotein expressed individually, partially translated into the Golgi, while the majority of this protein is localized in the endoplasmic reticulum (). However, when the G2 individually expressed, it becomes localized in the endoplasmic reticulum (;). It is important to note that the glycoprotein of the different hantaviruses able to interact resulting precise targeting to the Golgi complex ().

Viral infections fused innate immune response aimed at reducing viral replication. Type I interferon (IFN) plays an important role in providing antivirus protection directly and activate natural killer (NK) cells, the key effector cells of the innate immune response. On the other hand, in order to survive the virus develop a mechanism to prevent its removal by inhibiting type I IFN pathway activating transcription (;). It has been proven that the expression of the G1 protein cytoplasmic tail of pathogenic hantaviruses () inhibits the induction of IFN-β. This ability to distinguish pathogenic hantaviruses from the non-pathogenic, as the latter was not able to inhibit the induction of IFN-β (). G1 cytoplasmic tail of hantaviruses pathogen has been shown to inhibit the transcription of IFN-β by binding to TRAF3 () and preventing the RIG-I / TBK1-directed IRF3 phosphorylation (;). TRAF3 is E3 ubiquitin ligase that forms TBK1-TRAF3 complex, which is very important for IRF3 phosphorylation. Phosphorylation IRF3 very important in IFNβ induction.

reassortment, that is, the exchange of genome segments between the different virus strains, play an important role in maintaining a segmented virus and can produce new strains with characteristics of novel and improved survivability. Evolution of Rift Valley Fever virus (RVFV) presents an example of how new reassortants can be produced naturally in endemic areas (). rapid evolution of the virus that caused by reassortment can bring a global outbreak (;). Also, the ability to generate reassortants can put people living in endemic areas with the risk of producing a chimeric virus that is not controlled with the use of live attenuated vaccines (). Initially, genetic reassortment has proven among the members of the arthropod-borne Bunyaviridae (;). Then, genetic reassortment between strains of hantavirus different in nature have been documented as well (;). proposes that such reassortment can lead to the emergence of a new hantavirus strains with new epidemiological characteristics.

reassortment most likely to occur between the different genetic strains of hantavirus same, or between closely related hantaviruses circulating in rodent closely related host species. Although somewhat rare, reassortment between distantly related hantaviruses are also possible in nature. It is also known that hantavirus infection could “spill over” to host non-specific when different animal species share the same ecological niche. This could potentially lead to double infection of an animal. Replication two different hantaviruses in the same host organism can produce reassortants with new characteristics (;)

In vitro studies have shown that genetic reassortants can be developed between distantly related hantaviruses (;). In detail, the ability of two hantaviruses distantly related to developing reassortants in vitro has been investigated by. The authors suggest that ANDV and SNV (Figure) can generate new reassortants with different infectivity characteristics of both parent strains. Noteworthy, the resulting reassortant virus has always maintained the S and L segment of Hantavirus the same parents, whereas the M segment was introduced from the other. Apart from these two into Sigmodontinae-borne virus, rodent hosts they are separated geographically. SNV circulating in North America, while ANDV endemic to South America (). These data correspond to previously published findings by showing that heredity bunya reassortant virus containing between homologous segments S and L. Some breeds containing S and L segments that are heterozygous, that is, the virion containing the corresponding segments from both parental strains. Virus descendant of which is closely related hantaviruses have different prevalence of L homolog and S segment of people who are distantly related (;)

Hantavirus reassortment .. Infection of the host with two different strains of hantavirus can result in reassortment , Reassortment has been shown between ANDV and SNV resulted reassortants have ANDV M segment and SNV L and S segment.

Segment M plays an important role in the replication bunyavirus () and is also known to alter the efficiency of virus starters. Glycoprotein encoded by segment M take part in the annex to the cell surface, thus, they are essential for viral entry into host cells. It is interesting to note that steady descent reassortment between SNV and contained ANDV M segments of virus that has a higher capacity to replicate in the host cell type used in the experiment (). These data support the idea that the strategy used by viruses segmented reassortment can produce novel virus strains with higher capacity to deploy. Two conclusions additions which can be withdrawn from the trial reassortment is: (i) RdRp virus clearly works much better on template viral RNA coated with protein N homolog, and (ii) the cytoplasmic tail of hantavirus G1 / glycoprotein G2 seems to interact with the RNPs heterologous at least as efficiently with the homologous.

The ability to generate reassortants between distantly related hantaviruses provides a tool to study the roles of each segment of the virus (and corresponding virus protein) in the pathogenesis of infection. Also, reassortants can be used to analyze the specificity of hantavirus to the host animal.

hantavirus N protein consists of about 433 amino acid residues (about 50 kDa in size). N protein seems highly conserved among the different hantaviruses. It has been proven that a large amount of N protein is expressed early after infection (). Also, it has been demonstrated that early immune response in patients with Hantavirus is directed primarily against the N protein. Therefore, a lot of virus diagnostics developed based on detecting hantavirus N protein or anti-N protein antibody (;).

N protein expressed exclusively in the cytoplasm () from infected cells. Hantavirus N proteins play an important role in the viral life cycle as required for encapsidating RNA virus, as well as regulate viral replication and assembly.

N protein protects the viral genomic RNA from degradation by cellular nucleases by forming RNPs virus. RNA encapsidation mechanism is not fully understood. It has been proven that the N protein selectively interact with hantavirus RNA, encapsidating vRNA (genomic negative sense) and Crna (positive sense anti-genome) while leaving the mRNA virus free. selective encapsidation considered possible because of the unique structure protruding terminal formed by the free self terminal sequence of the full length vRNA and Crna. It has been demonstrated that this sequence of 23 nucleotides length of the terminal can serve as binding sites for the virus RdRp and has a high affinity for the protein N (). In particular, the N protein of several hantaviruses, as HTNV, has proven to be more binding on its S-vRNA segments than segments S open reading frame or non-specific RNA. This may indicate that the site Resides N protein recognition in the non-coding regions HTNV vRNA (). It was later reported that the binding depends on the sequence of the 5 ‘end of the vRNA segments S ().

It has been shown that replication efficiency Hantavirus is inversely proportional to the ability of infected cells to activate the MxA expression (). MxA protein is a key component of type I IFN-inducible antiviral state’s resistance to providing a variety of RNA viruses (). There are two types of human Mx protein, MxA and MXB (), with just MxA known to have anti-viral activity (). Interferon regulatory factor 3 (IRF-3) regulates transcriptional activation of genes MxA (). Generally, IRF-3 is present in the cytoplasm of cells in an active state (). However, after infection, IRF-3 translocates into the nucleus, where it initiate transcription of MxA and other IFN inducible genes (;). It has been proven that IRF-3 nuclear translocation can occur as early as 24 weeks after infection Hantavirus ().

MxA activation has proven to vary in different cell types (). For example, a high activation rate MxA demonstrated in human umbilical cord endothelial cells (HUVECs), while ativation of MxA in VeroE6 cells was nearly undetectable. Further studies have shown that the efficacy of hantavirus replication is inversely proportional to the ability of infected cells to activate the MxA protein expression (;). These data suggest that variation in hantavirus replication may partly depend on the ability of specific cell types to enable MxA protein. In turn, the MxA protein known to bind proteins form a complex protein MxA N / N (). Formation MxA / N complex has been suggested for some other bunya virus as a potential mechanism of inhibition of viral replication MxA (). , Thus, it is possible that in the case of MxA inhibition mechanism similar hantaviruses

The increase in microvascular permeability is characteristic for hantavirus infection (;;). However, the permeability of the endothelial cell monolayer unchanged after Hantavirus infection in vitro (;). Hantavirus infection is not cytopathic, therefore, it has been suggested that the increase in microvascular leakage is most likely related to the cell’s response to infection and not associated with viral replication. A DNA microarray is performed to determine changes in the cell’s response hantavirus-infected cells showed that non-pathogenic (PHV) and pathogens (SNV) hantaviruses have different effects on transcriptional activity in infected cells (). In particular, it has been demonstrated that infection activates PHV about five times fewer genes than not SNV infection (36 genes were up-regulated in PHV-infected cells compared with 175 genes in SNV-infected cells). As infection progresses, more change in the transcriptional activation is detected

Activation of nuclear factor and transcription proven vary in cells infected with pathogens than the non-pathogenic hantaviruses. (17 vs 8;). Also, hantavirus infection activates IRF-7, IRF-1 and IRF-9 transcription factor (). Interestingly, the transcriptional activity of these factors was lower in the non-pathogenic (PHV) than in pathogens (SNV) Hantavirus. Although no changes are recorded IRF3 transcriptional activity, nuclear translocation of these factors in hantavirus-infected cells was demonstrated by immunohistochemistry (). nuclear translocation IRF3 important for the activity which includes IFN-induced gene activation and cytokine activation. It has been demonstrated that IRF-3 activation control CCL5 gene transcription, whereas IRF-1 and IRF-3 regulates expression of MxA protein (). Up-regulation of CCL5 and MxA has been shown in hantavirus-infected cells. Therefore, it can be concluded that the activation induced hantavirus IRF1 and IRF3 can cause changes in cytokine and IFN-induced protein expression in infected cells.

Array DNA data have demonstrated upregulation of several genes control the process of apoptosis, growth and proliferation. For example, upregulation of Bcl-2 gene transcription activity has been detected in HUVECs infected with hantavirus. The cells also, Hantavirus infection is characterized by the activation of the transcription of vascular endothelial growth factor (VEGF), endothelial cell survival factor, preventing apoptosis by inducing the expression of Bcl-2. It has been proven that VEGF and Bcl-2 are working together to prevent apoptosis in vitro. For example, increased expression of Bcl-2 is found in neuroblastoma cells treated with VEGF. Also, VEGF abrogates apoptosis induced by TNF-α-induced serum starvation (;). Therefore, it can be suggested that the activation of Bcl-2 and VEGF may explain the presence of apoptosis in cells infected with hantavirus.

It has been suggested that cytokines play an important role in the pathogenesis of vascular leakage in hantavirus infection microvascular bed (). DNA Array Data have shown increased expression of a group of genes including CC chemokine RANTES (CCL5;). Also, the data presented by have shown that activation of transcription of CCL5 is characteristic for HTNV and PHV infection of endothelial cells. It is known that CCL5 plays a role in the regulation of immune effectors migration to the site of infection (). Interestingly, the accumulation of mononuclear leukocytes are characteristic histological hantavirus infection (). One can show that an increase in traffic of immune effectors through the monolayer of endothelial damage and, thus, making it more permeable ().

The expression of glycoproteins from pathogenic hantaviruses inhibits IFN-β and ICC -1 induction through the virulence determinants of the cytoplasmic tail are present on the G1. However, it has been suggested that, this alone may not be enough to make them virulent and several other virulence factors may play a role (). More recently, it has been shown that blocking the protein N ANDV autophosphorylation of TBK1 IRF3 resulted in inhibition of phosphorylation and RIG-I / kind MDA5-directed I IFN induction (). In addition, the N protein can affect the protein kinase R (PKR) dimerization (). It has been demonstrated that the protein hantavirus N prevent PKR phosphorylation, which is essential for enzymatic activity. PKR inhibits viral replication and is critical to establishing the state of antivirus (). PKR activate IFN through NF-kB and IRF1 up-regulation (). In addition, PKR can activate apoptosis in infected cells (). Therefore, it can be suggested that the glycoprotein and N protein can interfere with antiviral activity in infected cells, thus promoting viral replication.

There are two clinical entities associated with hantavirus infection, HFRS and HPS. The mortality rate can vary from 0.1 to 40% depending on the particular hantavirus involved. The hantavirus genome consists of three negative sense single-stranded RNA segments coding for the N protein, G1 and G2 glycoprotein and the viral polymerase. genetic reassortment between different hantaviruses have been documented both in nature and in vitro. reassortment as it could lead to the emergence of novel hantavirus strains with the virulence characteristics of the new and / or a new host range.

Emerging evidence suggests that hantavirus N protein plays a major role not only in viral replication, transcription, and virus assembly, but also in building a favorable environment for virus replication in host cells. pathogenic hantaviruses cause more obvious changes in transcriptional activity of various cellular genes compared to non-pathogenic strains. CCL5 activation may contribute to hantavirus-induced leukocyte accumulation in infected tissues and, potentially, to the pathogenesis of vascular permeability. The hantavirus N protein interacts with host proteins interfere with antiviral pathway activation in infected cells.

The authors state that the study was conducted in the absence of commercial or financial relations which can be construed as a potential conflict of interest.

This work was supported by the Russian Science Foundation grant 15-14-00016. the work is done in accordance with the Russian Government Program Growth Competitive Kazan Federal University and Kazan Federal University of subsidies allocated to the task of countries in the field of scientific activities.

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