Virus Host Cell Genetic Material Transport

2022 ◽  
Author(s):  
William E. Schiesser
Keyword(s):  
Host Cell ◽  
Genetic Material ◽  
Material Transport

scholarly journals Predicting mammalian hosts in which novel coronaviruses can be generated

2020 ◽  
Author(s):  
Maya Wardeh ◽  
Matthew Baylis ◽  
Marcus S.C. Blagrove
Keyword(s):  
High Risk ◽  
Homologous Recombination ◽  
Host Cell ◽  
Host Species ◽  
Genetic Material ◽  
Domesticated Animals ◽  
Host Interactions ◽  
Livestock Markets ◽  
Single Host ◽  
Novel Coronavirus

ABSTRACTNovel pathogenic coronaviruses – including SARS-CoV and SARS-CoV-2 – arise by homologous recombination in a host cell1,2. This process requires a single host to be infected with more than one type of coronavirus, which recombine to form novel strains of virus with unique combinations of genetic material. Identifying possible sources of novel coronaviruses requires identifying hosts (termed recombination hosts) of more than one coronavirus type, in which recombination might occur. However, the majority of coronavirus-host interactions remain unknown, and therefore the vast majority of recombination hosts for coronaviruses cannot be identified. Here we show that there are 11.5-fold more coronavirus-host associations, and over 30-fold more potential SARS-CoV-2 recombination hosts, than have been observed to date. We show there are over 40-fold more host species with four or more different subgenera of coronaviruses. This underestimation of both number and novel coronavirus generation in wild and domesticated animals. Our results list specific high-risk hosts in which our model predicts homologous recombination could occur, our model identifies both wild and domesticated mammals including known important and understudied species. We recommend these species for coronavirus surveillance, as well as enforced separation in livestock markets and agriculture.

scholarly journals Assessment of FTA card employment for Pasteurella multocida DNA transport and detection of virulence-associated genes in strains isolated from fowl cholera in the United States

2018 ◽  
Vol 70 (6) ◽  
pp. 1855-1861 ◽  
Author(s):  
C.N. Almeida ◽  
T.Q. Furian ◽  
K.A. Borges ◽  
G. Perdoncini ◽  
M.J. Mauel ◽  
...  
Keyword(s):  
United States ◽  
Pasteurella Multocida ◽  
Virulence Genes ◽  
Genetic Material ◽  
Storage Period ◽  
The United States ◽  
Material Transport ◽  
Dna Transport ◽  
Fowl Cholera ◽  
Fta Cards

ABSTRACT Fowl Cholera (FC) is a disease caused by Pasteurella multocida. The severity of this disease is partly caused by virulence factors. Genes encoding fimbriae, capsule, sialidases and proteins for iron metabolism may be related to P. multocida’s ability to infect the host. Besides to examining DNA for the presence of virulence genes, DNA is essential for the diagnostic and FTA cards are an alternative for genetic material transport. The study aims to evaluate the viability of P. multocida DNA transport using the cards and to detect 14 virulence genes in 27 strains isolated from FC cases in the United States by multiplex-PCR. No growth was observed in any of the FTA cards, which was essential to assess the security. Furthermore, DNA detection was possible in 100% of the samples, independent of the storage period (7 to 35 days) and temperature (4°C and 37°C). ptfA, exbd-tonB, hgbA, nanB, oma87, hyaD-hyaC, sodC, hgbB, sodA, nanH and pfhA genes were detected in more than 80% of the samples. FTA cards have proven to be a viable and safe tool for DNA transport of P. multocida. A majority of genes showed a high frequency, which was similar to strains isolated from FC cases.

scholarly journals Enzymes and Mechanisms Employed by Tailed Bacteriophages to Breach the Bacterial Cell Barriers

Viruses ◽  
2018 ◽  
Vol 10 (8) ◽  
pp. 396 ◽  
Author(s):  
Sofia Fernandes ◽  
Carlos São-José
Keyword(s):  
Cell Wall ◽  
Host Cell ◽  
Bacterial Cell ◽  
Cell Envelope ◽  
Genetic Material ◽  
Cell Types ◽  
Virus Multiplication ◽  
Virus Particles ◽  
Bacterial Cell Envelope ◽  
A Cell

Monoderm bacteria possess a cell envelope made of a cytoplasmic membrane and a cell wall, whereas diderm bacteria have and extra lipid layer, the outer membrane, covering the cell wall. Both cell types can also produce extracellular protective coats composed of polymeric substances like, for example, polysaccharidic capsules. Many of these structures form a tight physical barrier impenetrable by phage virus particles. Tailed phages evolved strategies/functions to overcome the different layers of the bacterial cell envelope, first to deliver the genetic material to the host cell cytoplasm for virus multiplication, and then to release the virion offspring at the end of the reproductive cycle. There is however a major difference between these two crucial steps of the phage infection cycle: virus entry cannot compromise cell viability, whereas effective virion progeny release requires host cell lysis. Here we present an overview of the viral structures, key protein players and mechanisms underlying phage DNA entry to bacteria, and then escape of the newly-formed virus particles from infected hosts. Understanding the biological context and mode of action of the phage-derived enzymes that compromise the bacterial cell envelope may provide valuable information for their application as antimicrobials.

scholarly journals DNA Aptamers Block the Receptor Binding Domain at the Spike Protein of SARS-CoV-2

2021 ◽  
Vol 8 ◽  
Author(s):  
Fabrizio Cleri ◽  
Marc F. Lensink ◽  
Ralf Blossey
Keyword(s):  
Host Cell ◽  
Low Cost ◽  
Protein A ◽  
Genetic Material ◽  
Dna Aptamers ◽  
Cell Binding ◽  
Host Cell Membrane ◽  
S Protein ◽  
Open Conformation ◽  
Viral Screening

DNA aptamers are versatile molecular species obtained by the folding of short single-stranded nucleotide sequences, with highly specific recognition capabilities against proteins. Here we test the ability of DNA aptamers to interact with the spike (S-)protein of the SARS-CoV-2 viral capsid. The S-protein, a trimer made up of several subdomains, develops the crucial function of recognizing the ACE2 receptors on the surface of human cells, and subsequent fusioning of the virus membrane with the host cell membrane. In order to achieve this, the S1 domain of one protomer switches between a closed conformation, in which the binding site is inaccessible to the cell receptors, and an open conformation, in which ACE2 can bind, thereby initiating the entry process of the viral genetic material in the host cell. Here we show, by means of state-of-the-art molecular simulations, that small DNA aptamers experimentally identified can recognize the S-protein of SARS-CoV-2, and characterize the details of the binding process. We find that their interaction with different subdomains of the S-protein can effectively block, or at least considerably slow down the opening process of the S1 domain, thereby significantly reducing the probability of virus-cell binding. We provide evidence that, as a consequence, binding of the human ACE2 receptor may be crucially affected under such conditions. Given the facility and low cost of fabrication of specific aptamers, the present findings could open the way to both an innovative viral screening technique with sub-nanomolar sensitivity, and to an effective and low impact curative strategy.

scholarly journals DNA Aptamers Block the Receptor Binding Domain at the Spike Protein of SARS-CoV-2

2020 ◽  
Author(s):  
Fabrizio Cleri ◽  
Marc F. Lensink ◽  
Ralf Blossey
Keyword(s):  
Host Cell ◽  
Low Cost ◽  
Protein A ◽  
Genetic Material ◽  
Dna Aptamers ◽  
Cell Binding ◽  
Host Cell Membrane ◽  
S Protein ◽  
Open Conformation ◽  
Viral Screening

<div> <div> <div> <p>DNA aptamers are versatile molecular species obtained by the folding of short single-stranded nucleotide sequences, with highly specific recognition capabilities against proteins. Here we test the ability of selected DNA aptamers in interacting with the spike (S-)protein of the SARS-CoV-2 viral capsid. The S-protein, a trimer made up of several subdomains, develops the crucial function of recognizing the ACE2 receptors on the surface of human cells, and sub- sequent fusioning of the virus membrane with the host cell membrane. In order to do this, the S1 domain of one protomer switches between a closed conformation, in which the binding site is inaccessible to the cell receptors, and an open conformation, in which ACE2 can bind, thereby initiating the entry process of the viral genetic material in the host cell. Here we show by means of state-of-the-art molecular simulations that small DNA aptamers can recognize the S-protein of SARS-CoV-2. Moreover, their interaction with different regions of the S-protein can effectively block, or at least considerably slow down the opening process of the S1 domain, thereby largely reducing the probability of virus-cell binding. We also provide evidence that binding of the human ACE2 receptor may be drastically affected under such conditions. Given the facility and low cost of fabrication of specific aptamers, the present findings could open the way to both an innovative viral screening technique with sub-nanomolar sensitivity, and to an effective and low impact curative strategy. </p> </div> </div> </div>

scholarly journals Pocket Factors Are Unlikely To Play a Major Role in the Life Cycle of Human Rhinovirus

2007 ◽  
Vol 81 (12) ◽  
pp. 6307-6315 ◽  
Author(s):  
Umesh Katpally ◽  
Thomas J. Smith
Keyword(s):  
Life Cycle ◽  
Host Cell ◽  
Cell Attachment ◽  
Limited Proteolysis ◽  
Genetic Material ◽  
Binding Pocket ◽  
Drug Binding ◽  
Human Rhinovirus ◽  
Mouth Disease Virus ◽  
Binding Cavity

ABSTRACT Human rhinovirus 14 (HRV14) is a member of the rhinovirus genus, which belongs to the picornavirus family, which includes clinically and economically important members, such as poliovirus, foot-and-mouth disease virus, and endomyocarditis virus. Capsid stability plays an important role in the viral infection process, in that it needs to be stable enough to move from cell to cell and yet be able to release its genetic material upon the appropriate environmental cues from the host cell. It has been suggested that certain host cell molecules, “pocket factors,” bind to the WIN drug-binding cavity beneath the canyon floor and provide transient stability to a number of the picornaviruses. To directly test this hypothesis, HRV14 was mutated in (V1188M, C1199W, and V1188M/C1199W) and around (S1223G) the drug-binding pocket. Infectivity, limited proteolysis, and matrix-assisted laser desorption ionization analyses indicate that filling the drug-binding pocket with bulky side chains is not deleterious to the viral life cycle and lends some stabilization to the capsid. In contrast, studies with the S1223G mutant suggest that this mutation at least partially overcomes WIN drug-mediated inhibition of cell attachment and capsid breathing. Finally, HRV16, which is inherently more stable than HRV14 in a number of respects, was found to “breathe” only at 37°C and did not tolerate stabilizing mutations in the drug-binding cavity. These results suggest that it is the drug-binding cavity itself and not the putative pocket factor that is crucial for the capsid dynamics, which is, in turn, necessary for infection.

scholarly journals DNA Aptamers Block the Receptor Binding Domain at the Spike Protein of SARS-CoV-2

2020 ◽  
Author(s):  
Fabrizio Cleri ◽  
Marc F. Lensink ◽  
Ralf Blossey
Keyword(s):  
Host Cell ◽  
Low Cost ◽  
Protein A ◽  
Genetic Material ◽  
Dna Aptamers ◽  
Cell Binding ◽  
Host Cell Membrane ◽  
S Protein ◽  
Open Conformation ◽  
Viral Screening

<div> <div> <div> <p>DNA aptamers are versatile molecular species obtained by the folding of short single-stranded nucleotide sequences, with highly specific recognition capabilities against proteins. Here we test the ability of selected DNA aptamers in interacting with the spike (S-)protein of the SARS-CoV-2 viral capsid. The S-protein, a trimer made up of several subdomains, develops the crucial function of recognizing the ACE2 receptors on the surface of human cells, and sub- sequent fusioning of the virus membrane with the host cell membrane. In order to do this, the S1 domain of one protomer switches between a closed conformation, in which the binding site is inaccessible to the cell receptors, and an open conformation, in which ACE2 can bind, thereby initiating the entry process of the viral genetic material in the host cell. Here we show by means of state-of-the-art molecular simulations that small DNA aptamers can recognize the S-protein of SARS-CoV-2. Moreover, their interaction with different regions of the S-protein can effectively block, or at least considerably slow down the opening process of the S1 domain, thereby largely reducing the probability of virus-cell binding. We also provide evidence that binding of the human ACE2 receptor may be drastically affected under such conditions. Given the facility and low cost of fabrication of specific aptamers, the present findings could open the way to both an innovative viral screening technique with sub-nanomolar sensitivity, and to an effective and low impact curative strategy. </p> </div> </div> </div>

scholarly journals Targeting mitotic chromosomes: a conserved mechanism to ensure viral genome persistence

2009 ◽  
Vol 276 (1662) ◽  
pp. 1535-1544 ◽  
Author(s):  
Katherine M Feeney ◽  
Joanna L Parish
Keyword(s):  
Host Cell ◽  
Genetic Material ◽  
Membrane Integrity ◽  
Mitotic Chromosomes ◽  
Nuclear Retention ◽  
Viral Genomes ◽  
Daughter Cells ◽  
Dna Damage Checkpoints ◽  
Low Copy Number ◽  
Dividing Cells

Viruses that maintain their genomes as extrachromosomal circular DNA molecules and establish infection in actively dividing cells must ensure retention of their genomes within the nuclear envelope in order to prevent genome loss. The loss of nuclear membrane integrity during mitosis dictates that paired host cell chromosomes are captured and organized by the mitotic spindle apparatus before segregation to daughter cells. This prevents inaccurate chromosomal segregation and loss of genetic material. A similar mechanism may also exist for the nuclear retention of extrachromosomal viral genomes or episomes during mitosis, particularly for genomes maintained at a low copy number in latent infections. It has been heavily debated whether such a mechanism exists and to what extent this mechanism is conserved among diverse viruses. Research over the last two decades has provided a wealth of information regarding the mechanisms by which specific tumour viruses evade mitotic and DNA damage checkpoints. Here, we discuss the similarities and differences in how specific viruses tether episomal genomes to host cell chromosomes during mitosis to ensure long-term persistence.

The Biology of Viruses

2019 ◽  
Author(s):  
Anna Jeffery-Smith ◽  
C. Y. William Tong
Keyword(s):  
Nucleic Acid ◽  
Host Cell ◽  
Genetic Material ◽  
Cell Types ◽  
Host Cells ◽  
Host Cell Membrane ◽  
Cell Receptors ◽  
A Cell ◽  
Independent Synthesis ◽  
Different Cell Types

In order to be classified as a virus, certain criteria have to be fulfilled. Viruses must ● Be only capable of growth and multiplication within living cells, i.e. obligate intracellular parasite. Host cells could include humans, animals, insects, plants, protozoa, or even bacteria. ● Have a nucleic acid genome (either RNA or DNA, but not both) surrounded by a protein coat (capsid). ● Have no semipermeable membrane, though some have an envelope formed of phospholipids and proteins. ● Be inert outside of the host cell. Enveloped viruses are susceptible to inactivation by organic solvents such as alcohol. ● Perform replication by independent synthesis of components followed by assembly (c.f. binary fission in bacteria). Viruses are considered as a bundle of genetic programmes encoded in nucleic acids and packaged with a capsid +/ - envelope protein, which can be activated on entry into a host cell (compare this with computer viruses packaged in an enticing way in order to infect and take over control of your PC). Although they share some similarities in their properties, mycoplasma and chlamydia are true bacteria. The virion (assembled infectious particle) consists of viral nucleic acid and capsid. The nucleic acid of a virus can either be ribonucleic acid (RNA) or deoxyribonucleic acid (DNA), and the amount of genetic material varies widely, with some viruses able to encode a few proteins and others having genetic material that encodes hundreds of proteins. In association with the nucleic acid there may be non- structural viral proteins, such as a viral polymerase. The nucleic acid and non- structural proteins are protected by a surrounding layer of capsid proteins. The capsid includes proteins which can attach to host cell receptors. The proteins and the cell receptors to which they bind determine a virus’ tropism, i.e., the ability to bind to and enter different cell types. The term nucleocapsid refers to the nucleic acid core surrounded by capsid protein. Some viruses also have an envelope made up of phospholipids and proteins surrounding the nucleocapsid. This envelope can be formed by the host cell membrane during the process of a virus budding from a cell during replication.

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