Parainfluenza virus entry at the onset of infection

Marcink, Tara C.; Porotto, Matteo; Moscona, Anne

doi:10.1016/bs.aivir.2021.07.001

Cited by 5 publications

(5 citation statements)

References 134 publications

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“…The pathogenesis of HPIV infections occurs by the spread through direct contact with infected droplets or through airborne transmission from an infected person's cough, breath, or sneeze. The virus attaches with the help of HN and F protein to and replicates in the ciliated epithelial cells of the upper and lower respiratory tracts and produces the symptoms [32].…”

Section: Discussionmentioning

confidence: 99%

In-silico multi-epitope vaccine candidate against type-1 parainfluenza virus

Khan

Sanjai

Sumera

et al. 2023

Preprint

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Human parainfluenza viruses (HPIV) are a group of viruses that cause different types of respiratory infections, most common in children and newborns. HPIV-1 (Human parainfluenza virus type-1) causes croup among children and can be quite severe. As there are no vaccines approved for HPIV infections, hence an In-silico approach was taken to construct a vaccine candidate against it. The HPIV-1 fusion glycoprotein antigen was chosen and subjected to B-cell and T-cell epitope prediction. The epitopes that passed the antigenicity, allergenicity, and toxicity profiles were chosen and for the construction of the vaccine, the B cell epitopes were linked with the peptide EAAAK, MHC-1 epitopes were linked with the peptide GPGPG, and MHC-2 epitopes were linked with the peptide AAY. Also, the adjuvant (50S ribosomal46 protein L7/L12) was added to the amino terminus for the vaccine to elicit a proper immune response. The tertiary structure prediction of the vaccine was done, and the structure was validated using Z-score and Ramachandran plot analysis, then the vaccine was docked with the TLR-8 receptor. The stability of the vaccine and TLR-8 docked complex was evaluated by molecular dynamic simulations. Finally, the reverse translated sequence of the vaccine was cloned with the pET-28a (+) vector. This could be a good initiative for the development of a vaccine against HPIV infections.

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Section: Discussionmentioning

confidence: 99%

In-silico multi-epitope vaccine candidate against type-1 parainfluenza virus

Khan

Sanjai

Sumera

et al. 2023

Preprint

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“…Respiratory viruses can be classified based on their nucleic acid composition: RNA viruses and DNA viruses. RNA viruses include influenza viruses A and B 13 , parainfluenza virus (PIV) 14 , human metapneumovirus (hMPV) 15 , respiratory syncytial virus (RSV; now known as human orthopneumovirus) 16 - 18 , coronaviruses 19 - 21 , and human rhinovirus (HRV) 22 . DNA viruses implicated in respiratory infections include adenoviruses (Adv) 23 , 24 and human bocavirus (HBoV) type 1 25 .…”

Section: Respiratory Pathogenic Microorganismsmentioning

confidence: 99%

Respiratory pathogenic microbial infections: a narrative review

Long,

Zheng,

et al. 2024

Int. J. Med. Sci.

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Respiratory infectious diseases have long been recognised as a substantial global healthcare burden and are one of the leading causes of death worldwide, particularly in vulnerable individuals. In the post COVID-19 era, there has been a surge in the prevalence of influenza virus A and other multiple known viruses causing cold compared with during the same period in the previous three years, which coincided with countries easing COVID-19 restrictions worldwide. This article aims to review community-acquired respiratory illnesses covering a broad spectrum of viruses, bacteria, and atypical microorganisms and focuses on the cluster prevalence of multiple known respiratory pathogens in China, thereby providing effective prevention and control measures.

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“…Structures of the soluble portion of individual paramyxovirus HN (or H or G) and F proteins have provided clues to the function of this HN/F fusion complex and led to conflicting models for the mechanism of action of the paramyxovirus fusion complex during entry (8,(15)(16)(17)(18), but the models agree that HN, upon receptor engagement, triggers the metastable, prefusion F to undergo the series of structural transitions that result in fusion of the viral and cellular membranes (1). Crystal structures of the soluble domains of receptor binding proteins are available for measles H; Nipah virus, Hendra virus, and respiratory syncytial virus G; and HPIV3, HPIV1, PIV5, and Newcastle disease virus (NDV) HNs and for the same viruses' fusion (F) proteins (6,(19)(20)(21)(22)(23)(24).…”

Section: Introductionmentioning

confidence: 99%

“…Enveloped viruses have evolved surface glycoprotein complexes that mediate fusion of their envelopes with their target cell and deliver the viral genome into the target cell cytoplasm. For the family Paramyxoviridae, which includes a broad swath of human pathogens, this complex consists of two membrane proteins that cooperate to mediate binding and cell entry ( 1 ). It has become clear that, for all these viruses—whether the receptor binding proteins bind sialic acid moieties, like parainfluenza virus, or proteinaceous receptors, like measles or Nipah viruses—upon receptor engagement, the receptor binding protein triggers the fusion protein to activate fusion and viral entry.…”

Section: Introductionmentioning

confidence: 99%

“…We previously showed that, on viral surfaces, HN and F were colocalized before receptor engagement ( 14 ). Cryo–electron tomography (cryo-ET) showed that HN was present in a canopy over the prefusion F in close association with F ( 1 , 7 ). In virions that were examined without disruptive purification steps, this HN canopy extends across the entirety of the virus’ surface, closely associated with prefusion F in the absence of target cell receptors and resting above F in what appears to be a possible mechanism for protecting F from activation ( 7 ).…”

Section: Introductionmentioning

confidence: 99%

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Subnanometer structure of an enveloped virus fusion complex on viral surface reveals new entry mechanisms

et al. 2023

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Paramyxoviruses—including important pathogens like parainfluenza, measles, and Nipah viruses—use a receptor binding protein [hemagglutinin-neuraminidase (HN) for parainfluenza] and a fusion protein (F), acting in a complex, to enter cells. We use cryo–electron tomography to visualize the fusion complex of human parainfluenza virus 3 (HN/F) on the surface of authentic clinical viruses at a subnanometer resolution sufficient to answer mechanistic questions. An HN loop inserts in a pocket on F, showing how the fusion complex remains in a ready but quiescent state until activation. The globular HN heads are rotated with respect to each other: one downward to contact F, and the other upward to grapple cellular receptors, demonstrating how HN/F performs distinct steps before F activation. This depiction of viral fusion illuminates potentially druggable targets for paramyxoviruses and sheds light on fusion processes that underpin wide-ranging biological processes but have not been visualized in situ or at the present resolution.

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Parainfluenza virus entry at the onset of infection

Cited by 5 publications

References 134 publications

In-silico multi-epitope vaccine candidate against type-1 parainfluenza virus

In-silico multi-epitope vaccine candidate against type-1 parainfluenza virus

Respiratory pathogenic microbial infections: a narrative review

Subnanometer structure of an enveloped virus fusion complex on viral surface reveals new entry mechanisms

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