Avian cells expressing the newcastle disease virus hemagglutinin-neuraminidase protein are resistant to newcastle disease virus infection

Morrison, Trudy G.; McGinnes, Lori W.

doi:10.1016/0042-6822(89)90505-9

Cited by 51 publications

(28 citation statements)

References 20 publications

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“…This mechanism of viral interference has been proposed to explain the interference phenomenon demonstrated for several paramyxoviruses (2,3,5). For NDV, Morrison et al (16) showed that the expression of cloned NDV HN resulted in resistance to subsequent infection by NDV; however, the mechanism of this interference mediated by HN remained unknown. In this report, we provide definitive evidence that the mechanism for attachment interference by a paramyxovirus is attributable to the viral neuraminidase enzyme, and we render proof of the mechanism of viral interference by HPF3.…”

Section: Discussionmentioning

confidence: 99%

“…A similar mechanism of interference via blockade of HN-binding sites on receptors could be considered for cellular expression of HPF3 HN; however, our results do not support this model since HPF3 neuramini- dase enzyme activity is essential for interference. In the case of influenza virus, which also makes use of sialic acid-containing receptors for entry, viral infection mediates interference; however, expression of the hemagglutinin (attachment) protein does not protect against viral infection (16), suggesting that receptor blockade is not important in the interference mechanism for influenza virus.…”

Section: Discussionmentioning

confidence: 99%

“…It has been shown by Morrison et al. that the expression of NDV HN results in resistance to viral infection by NDV (16). The question remains as to whether the resistance mediated by the expressed NDV HN was due to HN's neuraminidase activity.…”

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confidence: 98%

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Mechanism of Interference Mediated by Human Parainfluenza Virus Type 3 Infection

Horga

Gusella

Greengard

et al. 2000

J Virol

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Viral interference is characterized by the resistance of infected cells to infection by a challenge virus.Mechanisms of viral interference have not been characterized for human parainfluenza virus type 3 (HPF3), and the possible role of the neuraminidase (receptor-destroying) enzyme of the hemagglutinin-neuraminidase (HN) glycoprotein has not been assessed. To determine whether continual HN expression results in depletion of the viral receptors and thus prevents entry and cell fusion, we tested whether cells expressing wild-type HPF3 HN are resistant to viral infection. Stable expression of wild-type HN-green fluorescent protein (GFP) on cell membranes in different amounts allowed us to establish a correlation between the level of HN expression, the level of neuraminidase activity, and the level of protection from HPF3 infection. Cells with the highest levels of HN expression and neuraminidase activity on the cell surface were most resistant to infection by HPF3. To determine whether this resistance is attributable to the viral neuraminidase, we used a cloned variant HPF3 HN that has two amino acid alterations in HN leading to the loss of detectable neuraminidase activity. Cells expressing the neuraminidase-deficient variant HN-GFP were not protected from infection, despite expressing HN on their surface at levels even higher than the wild-type cell clones. Our results demonstrate that the HPF3 HN-mediated interference effect can be attributed to the presence of an active neuraminidase enzyme activity and provide the first definitive evidence that the mechanism for attachment interference by a paramyxovirus is attributable to the viral neuraminidase.Viral interference is defined as a state induced by an infecting virus that is characterized by the resistance of cells to subsequent infection by a challenge virus (7). Interference can be due to several different mechanisms, one of which is attachment interference. In this situation the interfering virus destroys or blocks the receptors for the superinfecting virus (7). Understanding mechanisms of viral interference can lead to strategies for controlling viral infection.The envelope of human parainfluenza virus type 3 (HPF3) contains two viral glycoproteins, the hemagglutinin-neuraminidase protein (HN) and the fusion protein (F). Infection of cells by HPF3 is initiated by attachment of the virus to the host cell through interaction of the HN glycoprotein with a sialic acid-containing cell surface receptor. Penetration and uncoating of the virus result from F protein-mediated fusion of the viral envelope with the plasma membrane of the cell, leading to the release of the viral nucleocapsid into the cytoplasm. In the case of HPF3 and other paramyxoviruses, HN as well as F are involved in membrane fusion, and cofunction of the HN and F glycoproteins was found to be necessary for syncytium formation (9, 10, 14, 17). Infection also results in fusion between cells, which involves the interaction of F and HN proteins expressed on the surface of an infected cell with the m...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Mechanism of Interference Mediated by Human Parainfluenza Virus Type 3 Infection

Horga

Gusella

Greengard

et al. 2000

J Virol

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“…NA assay: NA assay was carried out as described previously [3,18]. HEK-293 cells transfected with HN protein expression plasmids were washed twice in phosphate-buffered saline and once in phosphate buffer (PB, pH 5.9).…”

Section: Cells and Virusesmentioning

confidence: 99%

Increase in the Neuraminidase Activity of a Nonpathogenic Newcastle Disease Virus Isolate during Passaging in Chickens

Tsunekun

Ito

Kida

et al. 2010

The Journal of Veterinary Medical Science

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ABSTRACT. A pathogenic mutant of the Newcastle disease virus (NDV) was previously generated by passaging a non-pathogenic isolate from wild waterfowl. Velogenic mutant 9a5b (IVPI=2.67) contains three amino acid substitutions (128H, 495K and 573stop) in the hemagglutinin-neuraminidase (HN) protein, as compared with nonpathogenic waterfowl isolate 415/91 strain, and two of these (128H and 495K) were introduced after mesogenic 9a3b (IVPI=1.88). To investigate the role of the HN protein in NDV virulence, the function of HN protein such as neuraminidase (NA), Hemadsorption (HAd) and fusion promotion activities was examined by introducing the point mutations observed in passaged mutants into the HN gene cDNAs. In vitro functional assay using mutant protein expression demonstrated that the 128H substitution markedly increases NA activity and 573stop substitution increase NA and HAd activities. On the other hand, 495K substitution had little effect on any activities. These results indicate that a single amino acid substitution (128P to H) in the NDV HN protein affects the neuraminidase activity and is possibly correlated with the virulence.KEY WORDS: hemagglutinin-neuraminidase protein, IVPI, Newcastle disease virus, passage, pathogenicity.J. Vet. Med. Sci. 72(4): 453-457, 2010 Newcastle disease virus (NDV) is classified as a member of the genus Avulavirus, belonging to the family Paramyxoviridae [12,16]. It causes a highly contagious respiratory, neurological or enteric disease in all species of birds, and is responsible for significant economic losses in the commercial poultry industry worldwide. Strains of NDV can be differentiated on the basis in their pathogenicity in chickens into strains of high (velogenic), intermediate (mesogenic) and low (lentogenic) virulence [1,2,24].NDV has two surface glycoproteins, a fusion (F) protein and a hemagglutinin-neuraminidase (HN) protein [11]. The F protein mediates fusion of the virion envelope with the cellular plasma membrane. It is synthesized as an inactive precursor, F 0 , which must be proteolytically cleaved to form a disulfide-linked heterodimer of F 1 and F 2 in order to activate membrane fusion activity. The F proteins of virulent strains differ from those of avirulent strains with regard to the presence of a pair of dibasic amino acids at the carboxyl (C) terminus of F 2 [5,20,22]. Whereas the F protein of virulent strains is cleaved by furin or other ubiquitous intracellular host cell proteases, the F protein of avirulent strains is cleaved by trypsin-like enzymes found in limited tissue. As a result, avirulent strains can only replicate in areas with trypsin-like enzymes, such as the respiratory and intestinal tracts, whereas virulent strains can replicate in a range of tissues and organs, resulting in fatal systemic infection [20,21].The HN protein possesses both the receptor recognition and neuraminidase (NA) activities associated with the virus. It is responsible for the attachment of virus particles to sialic acid-containing receptors of the host cell, it p...

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“…Unbound red blood cells were washed away, bound red blood cells were lysed in 0.05 M NH4Cl, and the hemoglobin released was measured as the optical density at 549 nm. 24) Neuraminidase assay. Neuraminidase activity of HN proteins on the cell surface was measured by a ‰uorometric procedure.…”

Section: )mentioning

confidence: 99%

Functional Analysis of Individual Oligosaccharide Chains of Sendai Virus Hemagglutinin-neuraminidase Protein

Segawa

Inakawa

Yamashita

et al. 2003

Bioscience, Biotechnology, and Biochemistry

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Avian cells expressing the newcastle disease virus hemagglutinin-neuraminidase protein are resistant to newcastle disease virus infection

Cited by 51 publications

References 20 publications

Mechanism of Interference Mediated by Human Parainfluenza Virus Type 3 Infection

Mechanism of Interference Mediated by Human Parainfluenza Virus Type 3 Infection

Increase in the Neuraminidase Activity of a Nonpathogenic Newcastle Disease Virus Isolate during Passaging in Chickens

Functional Analysis of Individual Oligosaccharide Chains of Sendai Virus Hemagglutinin-neuraminidase Protein

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