Bovine herpesvirus type 1 gp87 mediates both attachment of virions to susceptible cells and hemagglutination

Okazaki, Katsunori; Honda, Eichi; Minetoma, Toshimi; Kumagai, Tomohisa

doi:10.1007/bf01314428

Cited by 24 publications

(9 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…These results strongly confirm our previous finding that the hemagglutinin subunit might be associated with a 59 kDa gp [4]. Consequently, it appears that the FHV-1 hemagglutinin also includes an important VN epitope, just as the bovine herpesvirus type 1 hemagglutinin has been identified to be the protein responsible for attachment to susceptible cell [8].…”

supporting

confidence: 90%

Feline herpesvirus type 1 glycoproteins eliciting virus neutralizing and hemagglutination-inhibiting antibodies

Horimoto

Limcumpao

Tohya

et al. 1990

Archives of Virology

View full text Add to dashboard Cite

Monoclonal antibodies (MoAbs) to feline herpesvirus type 1 (FHV-1) were produced to identify the virus-specified immunogenic proteins. When antigens recognized by the MoAbs were investigated by immunoblot and immunoprecipitation assays using FHV-1-infected cell lysate, four groups of immunogenic proteins were identified. MoAbs directed against 60 kDa, 113 kDa, and 143 kDa/108 kDa glycoproteins had virus neutralizing activities, but those against 170 kDa protein did not. Furthermore, MoAbs to the 60 kDa glycoprotein also showed hemagglutination-inhibition activity, indicating that this glycoprotein might be the hemagglutinin.

show abstract

supporting

confidence: 90%

Feline herpesvirus type 1 glycoproteins eliciting virus neutralizing and hemagglutination-inhibiting antibodies

Horimoto

Limcumpao

Tohya

et al. 1990

Archives of Virology

View full text Add to dashboard Cite

show abstract

“…These findings suggest that N polypeptide of PRRSV is playing an extrimely important role in HA activity of PRRSV. Although elucidation of the mechanisms of HA activity of PRRSV will be required in the further studies, it is worthy of note that the HAin of PRRSV is strikingly different from those of orthomyxoviruses, paramyxoviruses and herpesviruses, which are considered to be a part of virion envelope responsible for adsorption of the viruses on the host cells to initiate virus infection (3,6,8,14,18,22).…”

Section: Discussionmentioning

confidence: 99%

“…The disease is characterized by severe reproductive failure in sows and gilts, pneumonia in nursery and young growing pigs, and an increase in preweaning mortality [2,12,15,18]. We have reported that PRRSV agglutinates mouse erythrocytes and the hemagglutination (HA) reaction is inhibited by specific antiserum [4].…”

mentioning

confidence: 99%

Characterization of Porcine Reproductive and Respiratory Syndrome Virus Hemagglutinin.

Jusa¹,

Inaba

Kouno³

et al. 1997

J. Vet. Med. Sci.

View full text Add to dashboard Cite

ABSTRACT. Porcine reproductive and respiratory syndrome virus hemagglutinin (HAin) was readily adsorbed on mouse erythrocytes at 4, 22, or 37°C, but not on goose erythrocytes. The adsorbed HAin could not be eluted from the cells by resuspending in phosphate buffered saline, by incubating at 37 or 50°C, or by incubating in the presence of neuraminidase. The hemagglutinating activity was not dependent on the pH and NaCl molarity tested. The receptor of mouse erythrocytes for the HAin was relatively stable to trypsin, neuraminidase, sodium deoxycholate (DOC), potassium periodate (KIO 4 ), dithiothreitol (DTT), 2-mercaptoethanol (2-ME) and formalin treatments. The HAin was inactivated by 2-ME and was gradually inactivated by pepsin, formalin and DTT, but not by β-glucosidase, trypsin, α-amylase, papain, phospholipase C, neuraminidase, KIO 4 , and ethylendiamine tetraacetic acid (EDTA) treatments. The HAin was stable at 37°C or lower temperatures, but not at 56°C or higher. The HAin was relatively resistant to ultraviolet irradiation and sonication. In the equilibrium centrifugation of the HAin preparation on a CsCl density gradient, the HAin activity showed a sharp peak at 1.17 g/cm 3 . In the SDS-PAGE analysis, the structural polypeptide of HAin in the peak fraction seems to be the nucleocapsid (N) polypeptide with molecular weight of 15 kDa. bovine serum albumin (BSA; Fraction V) and antibiotics as above. Preparation of HAin:The HAin was prepared by the method described previously [4], with slight modification. Briefly, the infected culture fluid of MARC-145 cells was concentrated by adding 2% of 1 M zinc acetate solution and adjusted to pH 7.2 with 1 M NaOH. The mixture was stirred constantly at 4°C for 1 hr. After low-speed centrifugation the pellet was suspended in 1/50 the original volume of saturated solution of ethylenediamine tetraacetic acid (EDTA), adjusted to pH 7.2 by the addition of solid Tris (hydroxymethyl) aminomethane (Wako, Japan). The resulting solution was clarified by low-speed centrifugation and the supernatant was layered on 20% (w/v) sucrose solution and centrifuged at 100,000 × g for 4 hr (SW40Ti rotor Beckman, U.S.A.). The pellet was resuspended in 1/ 100 the original volume of PBS (0.15 M NaCl, 0.02 M phosphate buffer, pH 7.2) containing 0.2% BSA (PBS-BA) and then pretreated with 0.06% (v/v) of Tween 80 followed by 50% (v/v) of ether (Diethylether, Wako, Japan). The aqueous phase was used as HAin after the remaining of ether was sacked off and discarded. The HAin was stored at 4°C or 80°C before used.Preparation of pig immune serum: A 13-day-old pig obtained from the specific-pathogen-free farm was inoculated intranasally with 10 3.5 TCID 50 of the EDRD-1 strain of PRRSV grown on primary porcine alveolar macrophages. Serum samples were taken immediately before inoculation and at 6 weeks after inoculation for immunoblotting assay.HA test: HA test was carried out by microtiter method using ddY mouse erythrocytes as described previously [4].

show abstract

“…It has been reported that the gIII of bovine herpesvirus type 1 [14,16] and the gp60 of feline herpesvirus type 1 [7,8] are their respective hemagglutinins, and that they also contain important epitopes for virus neutralization. Previously, we demonstrated CHV-specific hemagglutination activity against dog erythrocyte [12].…”

Section: Discussionmentioning

confidence: 99%

Neutralizing determinants of canine herpesvirus as defined by monoclonal antibodies

Xuan

Horimoto

Limcumpao

et al. 1991

Archives of Virology

View full text Add to dashboard Cite

Monoclonal antibodies (MoAbs) against canine herpesvirus (CHV) were produced to identify the immunogenic proteins of the virus carrying neutralizing determinants. A panel of 24 MoAbs showing neutralizing activities was obtained and tentatively classified into 3 different groups based on their reactivity patterns in immunoblotting analysis. Group I consisting of 10 clones was specific for 145/112 kDa; Group II of 9 clones, for 80 kDa; and Group III of 5 clones, for 41 kDa glycoproteins (gps). Complement-requirement for neutralizing activities of the MoAbs suggests that gp 145/112 and gp 80 elicit mainly complement-requiring and -enhanced neutralizing antibodies, while gp 41 elicits complement-independent ones. In addition, these MoAbs were used in ELISA additivity tests for functional and topographical mapping of epitopes in each of the CHV gp. The results indicated that antigenic reactivities of gp 145/112 and gp 80 were, respectively, localized on at least 5 and 7 overlapping epitopes. On the other hand, 4 epitopes were identified on gp 41.

show abstract

Bovine herpesvirus type 1 gp87 mediates both attachment of virions to susceptible cells and hemagglutination

Cited by 24 publications

References 37 publications

Feline herpesvirus type 1 glycoproteins eliciting virus neutralizing and hemagglutination-inhibiting antibodies

Feline herpesvirus type 1 glycoproteins eliciting virus neutralizing and hemagglutination-inhibiting antibodies

Characterization of Porcine Reproductive and Respiratory Syndrome Virus Hemagglutinin.

Neutralizing determinants of canine herpesvirus as defined by monoclonal antibodies

Contact Info

Product

Resources

About