Effects of specific monoclonal antibodies on La crosse virus neutralization: Aggregation, inactivation by Fab fragments, and inhibition of attachment to baby hamster kidney cells

Kingsford, Laura; Boucquey, Kristin H.; Cardoso, Tamre Porter

doi:10.1016/0042-6822(91)90073-k

Cited by 14 publications

(12 citation statements)

References 34 publications

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“…4). These results show that there is an imperfect relationship between in vitro neutralization and in vivo protective ability, at least under the assay conditions used here, and that the ability of an antibody to neutralize CCHFV may depend in part on host factors, as has been observed for La Crosse virus (LACV), another bunyavirus (25)(26)(27).…”

Section: Virus Neutralization and Protection Studiesmentioning

confidence: 88%

“…A number of MAbs against G C , but not against G N , were able to neutralize virus infection of SW-13 cells in vitro, suggesting that G C plays an important role in virus entry. Similarly, MAbs directed against the G C glycoproteins of LACV can inhibit virus infection, with some evidence indicating that this is due to a reduction in virus binding to the cell surface (19,21,22,26). However, some antibodies against G N can neutralize LACV infection in an insect cell line, though not in a mammalian cell line, suggesting that virus neutralization can be dependent on the cell type being infected and that virus entry mechanisms may differ between invertebrates and vertebrates (30).…”

Section: Discussionmentioning

confidence: 99%

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Cellular Localization and Antigenic Characterization of Crimean-Congo Hemorrhagic Fever Virus Glycoproteins

Bertolotti-Ciarlet

Smith

Strecker

et al. 2005

J Virol

148

202

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Crimean-Congo hemorrhagic fever virus (CCHFV), a member of the genus Nairovirus of the family Bunyaviridae, causes severe disease with high rates of mortality in humans. The CCHFV M RNA segment encodes the virus glycoproteins GN and GC. To understand the processing and intracellular localization of the CCHFV glycoproteins as well as their neutralization and protection determinants, we produced and characterized monoclonal antibodies (MAbs) specific for both GN and GC. Using these MAbs, we found that GN predominantly colocalized with a Golgi marker when expressed alone or with GC, while GC was transported to the Golgi apparatus only in the presence of GN. Both proteins remained endo-β-N-acetylglucosaminidase H sensitive, indicating that the CCHFV glycoproteins are most likely targeted to the cis Golgi apparatus. Golgi targeting information partly resides within the GN ectodomain, because a soluble version of GN lacking its transmembrane and cytoplasmic domains also localized to the Golgi apparatus. Coexpression of soluble versions of GN and GC also resulted in localization of soluble GC to the Golgi apparatus, indicating that the ectodomains of these proteins are sufficient for the interactions needed for Golgi targeting. Finally, the mucin-like and P35 domains, located at the N terminus of the GN precursor protein and removed posttranslationally by endoproteolysis, were required for Golgi targeting of GN when it was expressed alone but were dispensable when GC was coexpressed. In neutralization assays on SW-13 cells, MAbs to GC, but not to GN, prevented CCHFV infection. However, only a subset of GC MAbs protected mice in passive-immunization experiments, while some nonneutralizing GN MAbs efficiently protected animals from a lethal CCHFV challenge. Thus, neutralization of CCHFV likely depends not only on the properties of the antibody, but on host cell factors as well. In addition, nonneutralizing antibody-dependent mechanisms, such as antibody-dependent cell-mediated cytotoxicity, may be involved in the in vivo protection seen with the MAbs to GC

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Section: Virus Neutralization and Protection Studiesmentioning

confidence: 88%

Section: Discussionmentioning

confidence: 99%

Cellular Localization and Antigenic Characterization of Crimean-Congo Hemorrhagic Fever Virus Glycoproteins

Bertolotti-Ciarlet

Smith

Strecker

et al. 2005

J Virol

148

202

View full text Add to dashboard Cite

show abstract

“…However, HC10 neutralizes mainly by means other than aggregation , and it is not known how its Fabs neutralize. In category (v) are certain Fabs to sites B and C of La Crosse virus that neutralized to a greater extent or at a faster rate than did their respective IgGs (Kingsford et al, 1991). However, the affinities of these Fabs and their IgGs are not known, so no further interpretation is possible.…”

Section: F(abh) 2 S and Fabs Of Influenza And Other Virusesmentioning

confidence: 99%

“…However, neutralization by a Fab is usually reduced by at least an order of magnitude compared with its IgG, and often by much more. Exceptions are certain Fabs to La Crosse virus (Bunyaviridae) site B and site C which neutralized to a greater extent or faster rate than did their respective monoclonal IgGs (Kingsford et al, 1991). From limited studies it seems that the affinity of a Fab preparation is usually decreased over that of its IgG.…”

Section: Introductionmentioning

confidence: 99%

Variations in the neutralizing and haemagglutination-inhibiting activities of five influenza A virus-specific IgGs and their antibody fragments.

Schofield

Stephenson

Dimmock

1997

Journal of General Virology

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Neutralization and haemagglutination-inhibition (HI) of a type A influenza virus by a panel of five monoclonal IgGs, their F(abh) 2 s, Fabs and FabsM anti-mouse Fab were compared. The MAbs were specific for antigenic sites A, B and D of the haemagglutinin. Activities of the IgGs varied by up to 6-fold on a molar basis, apart from the HI activity of HC58 which was 100-fold lower. This was not due to low functional affinity as HC58 had the second highest value (nM) as determined by an equilibrium method with whole virions. Conversion to the F(abh) 2 reduced neutralization and HI by only 2-to 6-fold, indicating that the Fc region had little involvement in these processes. However, all Fabs had low neutralization and HI activity compared with their IgGs, neutralization being reduced by 86

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“…The mechanisms of neutralization of members of the Bunyaviridae by antibody have been examined previously (Green et al, 1992 ;Kingsford et al, 1991 ;Pekosz et al, 1995), but not as quantitatively as with some other viruses (Icenogle et al, 1983 ;Taylor et al, 1987). For example, poliovirus requires an average of four bound antibodies per virion (out of approximately 30 potential antibody-binding sites on each particle) to reduce the titre to 1\e of its original value (Icenogle et al, 1983).…”

Section: Co-infection (A)mentioning

confidence: 99%

Pseudotype formation with La Crosse virus glycoproteins.

Bupp

González‐Scarano

1998

Journal of General Virology

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Pseudotype formation is a powerful tool for analysing mechanisms of virus neutralization and entry, since it allows for analysis of glycoprotein properties without the necessity for preparing recombinant genomes. Using recombinant vaccinia viruses, we prepared pseudotypes of La Crosse virus with recombinant glycoproteins cloned from the monoclonal antibody (MAb)-resistant variant V31. The resulting pseudotypes became partially resistant to MAb 807-31. Furthermore, when the V31 glycoproteins were incorporated into a second MAb-resistant variant (V33), the pseudotyped virus became sensitive to neutralization by the MAb (807-33) originally used in its selection. These results suggest a simple technique for the incorporation of glycoprotein mutations into bunyaviruses, allowing analysis of mechanisms of neutralization and other virus entry functions.La Crosse virus (LAC) is a member of the California serogroup of the genus Bunyavirus of the family Bunyaviridae, and like all members of the family has a tri-segmented genome with segments designated L (large), M (medium) and S (small). The L RNA segment encodes the L or polymerase protein. The M segment encodes a single open reading frame that is processed into the two viral glycoproteins G1 and G2, as well as NSm -a non-structural protein of unknown function. The S segment encodes the nucleocapsid protein and another nonstructural protein (NSs) in overlapping reading frames (Elliott, 1990).The G1 and G2 glycoproteins of LAC have been expressed using vaccinia virus (VV) vectors. Several of the glycoprotein functions, such as targeting to the Golgi apparatus (a characteristic of bunyaviruses) and pH-dependent fusogenicity, are faithfully reproduced by the recombinant proteins (Bupp et

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Effects of specific monoclonal antibodies on La crosse virus neutralization: Aggregation, inactivation by Fab fragments, and inhibition of attachment to baby hamster kidney cells

Cited by 14 publications

References 34 publications

Cellular Localization and Antigenic Characterization of Crimean-Congo Hemorrhagic Fever Virus Glycoproteins

Cellular Localization and Antigenic Characterization of Crimean-Congo Hemorrhagic Fever Virus Glycoproteins

Variations in the neutralizing and haemagglutination-inhibiting activities of five influenza A virus-specific IgGs and their antibody fragments.

Pseudotype formation with La Crosse virus glycoproteins.

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