Amino acid change 335 E to K affects the sialic-acid-binding and neuraminidase activities of Urabe AM9 mumps virus hemagglutinin–neuraminidase glycoprotein

Reyes‐Leyva, Julio; Baños, Rocı́o; Borraz-Argüello, M. T.; Santos‐López, Gerardo; Rosas, Nora; Alvarado, Gabriela; Herrera, I.G. Salas; Vallejo, Verónica; Tapia-Ramı́rez, José

doi:10.1016/j.micinf.2006.11.011

Cited by 22 publications

(26 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…This type of sialic acid is abundantly exposed on the membrane surface of human neuroblastoma cells, facilitating HN-K 335 virus entry into the cells. Additionally, HN-K 335 virus has 11 times higher neuraminidase activity than does HN-E 335 , contributing to virus release [13].…”

mentioning

confidence: 99%

Structure-function analysis of two variants of mumps virus hemagglutinin-neuraminidase protein

Santos‐López¹,

Scior²,

Borraz-Argüello³

et al. 2009

Braz J Infect Dis

Self Cite

View full text Add to dashboard Cite

A point mutation from guanine (G) to adenine (A) at nucleotide position 1081 in the hemagglutinin-neuraminidase (HN) gene has been associated with neurovirulence of Urabe AM9 mumps virus vaccine. This mutation corresponds to a glutamic acid (E) to lysine (K) change at position 335 in the HN glycoprotein. We have experimentally demonstrated that two variants of Urabe AM9 strain (HN-A 1081 and HN-G 1081 ) differ in neurotropism, sialic acidbinding affinity and neuraminidase activity. In the present study, we performed a structure-function analysis of that amino acid substitution; the structures of HN protein of both Urabe AM9 strain variants were predicted. Based on our analysis, the E/K mutation changes the protein surface properties and to a lesser extent their conformations, which in turn reflects in activity changes. Our modeling results suggest that this E/K interchange does not affect the structure of the sialic acid binding motif; however, the electrostatic surface differs drastically due to an exposed short alpha helix. Consequently, this mutation may affect the accessibility of HN to substrates and membrane receptors of the host cells. Our findings appear to explain the observed differences in neurotropism of these vaccine strains.

show abstract

mentioning

confidence: 99%

Structure-function analysis of two variants of mumps virus hemagglutinin-neuraminidase protein

Santos‐López¹,

Scior²,

Borraz-Argüello³

et al. 2009

Braz J Infect Dis

Self Cite

View full text Add to dashboard Cite

show abstract

“…Some virological studies supported this finding [21,22]. However, the complete nucleotide sequences of several stocks of the Urabe strain did not support this finding [34,35], and reverse genetic work finally showed that HN 335 was not a crucial determinant of Urabe neurovirulence [36].…”

Section: Discussionmentioning

confidence: 95%

“…The virulence of MuV has recently been studied using the reverse genetic techniques established for Jeryl Lynn strain cDNA [17]. The genetic basis for attenuation has been vigorously studied [18][19][20][21][22][23], but a common genetic factor for MuV attenuation has not yet been identified.…”

Section: Open Accessmentioning

confidence: 99%

Comparison of the live attenuated mumps vaccine (Miyahara strain) with its preattenuated parental strain

Nagata¹,

Maedera²,

Nagata³

et al. 2013

J Vaccines Immun

View full text Add to dashboard Cite

“…Recientemente nuestro grupo ha reportado un proceso similar en la infección de dos clonas obtenidas de la cepa vacunal Urabe AM9 del virus de la parotiditis (Santos-López et al 2006, Reyes-Leyva et al 2007. Una de las clonas virales, denominada HN-G 1081 , induce un mayor nivel de fusión celular en células Vero (riñón de mono) y posee un más bajo nivel de neuraminidasa que la otra clona denominada HN-A 1081 .…”

Section: Discussionunclassified

“…Los sedimentos se re-suspendieron en PBS (fosfato de sodio 0.1 M (Sigma)/cloruro de sodio 0.15 M (Sigma), pH 7.3) y se sometieron a ultracentrifugación a 100,000xg/4 hr/4ºC en un colchón de sacarosa (Sigma) al 45% usando el rotor SW-28 (Beckman, Palo Alto, E.U.A.). Los viriones sedimentados se lavaron con PBS mediante otra centrifugación a 31,000xg/l hr/4 °C, se resuspendieron en PBS y se guardaron a -70 ºC hasta su uso (Reyes-Leyva et al 2007). …”

Section: Purificación De Virusunclassified

Caracterización biológica de tres aislamientos naturales del Rubulavirus porcino (México)

Borraz-Argüello¹,

Santos‐López²,

Vallejo-Ruíz³

et al. 2007

RBT

View full text Add to dashboard Cite

Biological characterization of three natural isolates of the porcine rubulavirus (Mexico).Porcine rubulavirus (PoRV) produces a neurological and reproductive syndrome in pigs called the blue-eye disease, known only from Mexico. Several isolates were grouped by the main symptoms presented during outbreaks: a) neurotropic in piglets, b) broadly neurotropic in piglets and gonadotropic in adults, and c) gonadotropic in adults. We studied some biological properties of three strains, which fall in one of each virus group: La Piedad Michoacán (LPM) and Producción Animal Cerdos 1 (PAC1) and 3 (PAC3), respectively. The analyzed viral properties are mainly related with the trans-membrane hemagglutinin-neuraminidase (HN) and fusion (F) proteins, such as cytopathic effect, hemolysis, hemagglutinating (HA) and neuraminidase (NA) activities. In the infection assays PAC1 strain presented the highest fusogenicity level; however, the most cytolytic strain was PAC3. In addition, HA and NA activities and viral genome of PAC3 strain was detected in supernatants during cell infection earlier than in the other two strains, which shows that PAC3 virions release from the host cell earlier than LPM and PAC1. Experimental determination in purified viruses shows that PAC3 presented a higher HA and NA activities; however, PAC1 shows other interesting properties, such as a high thermostability of HN and differences about substrate profile respect to LPM and PAC3. Our data suggest that NA activity is associated with the virulence of RVP. Rev. Biol. Trop. 56 (2): 487-499. Epub 2008 June 30.

show abstract

Amino acid change 335 E to K affects the sialic-acid-binding and neuraminidase activities of Urabe AM9 mumps virus hemagglutinin–neuraminidase glycoprotein

Cited by 22 publications

References 27 publications

Structure-function analysis of two variants of mumps virus hemagglutinin-neuraminidase protein

Structure-function analysis of two variants of mumps virus hemagglutinin-neuraminidase protein

Comparison of the live attenuated mumps vaccine (Miyahara strain) with its preattenuated parental strain

Caracterización biológica de tres aislamientos naturales del Rubulavirus porcino (México)

Contact Info

Product

Resources

About