Measles Virus

Background

Measles virus (Measles morbillivirus) is an enveloped, single-stranded, negative-sense RNA virus belonging to the genus Morbillivirus of the family Paramyxoviridae. The virus is highly contagious and spreads primarily through respiratory aerosol droplets. In unvaccinated populations, measles is usually acquired during childhood due to the high infectivity of the virus. Measles virus infection causes cold-like symptoms, fever, characteristic Koplik spots and maculopapular rash which spreads form the head to the trunk and lower extremities. Measles infection may be fatal even in children, which is often due to a measles-induced immunosuppression and subsequent opportunistic secondary infections [1]. Despite vaccination since the 1960s, infections still appear worldwide, even in the U.S., where measles was declared eliminated in 2000 [2].

Antigens

SERION Immunologics offers the native Measles Virus Antigen - Premium (BA102VS-S) and the recombinant Measles Virus Nucleoprotein (BA102R01).

The native Measles Virus Antigen – Premium (BA102VS-S) is produced by cultivation of measles virus (strain Edmonston) in Vero cells and a subsequent concentration of the culture supernatant by ultra-filtration and ultra-centrifugation. The resulting antigen preparation consists of a high concentration of virus and viral components that enable very sensitive and specific detection of IgG and IgM antibodies.

For the development of chemiluminescence immunoassays (CLIA), where antigens are usually immobilized by covalent coupling to reactive groups on microparticles or other solid phases, recombinant antigens are often the first choice. Although antigens purified from their native sources can be coupled successfully as well, recombinant antigens often show a better and more reliable performance in chemical coupling procedures. The recombinant Measles Virus Nucleoprotein (BA102R01) is expressed in insect cells and highly purified by strep-tag affinity chromatography. It comprises the viral nucleoprotein, which is the most abundant of the viral proteins. Multiple copies bind the RNA and form the helical nucleocapsid [3]. Likewise, the recombinant nucleoprotein BA102R01 assembles in nucleocapsid-like particles about 20 nm in diameter (see figure 1). During infection, viral nucleoprotein is synthesized in the cytoplasm of infected cells and secreted [4]. In terms of immune response, the nucleocapsid can contribute to measles-induced immunosuppression [5], [6], but it is also a target for B- and T-cell responses [7]. Hence, nucleoprotein is very well suited for the application in infectious serology.

Please let us know if you are interested in 0.25 mg test samples.

Figure 1:Three independent production batches of recombinant Measles Virus Nucleoprotein (BA102R01) were analyzed by dynamic light scattering (DLS). The determined hydrodynamic diameter was 22.16 nm ± 1.74. Detected aggregates were < 1 % (peak area by volume).

References:

[1] M. J. Mina, C. J. E. Metcalf, R. L. de Swart, A. D. M. E. Osterhaus, and B. T. Grenfell, “Long-term measles-induced immunomodulation increases overall childhood infectious disease mortality,” Science, vol. 348, no. 6235, pp. 694–699, May 2015, doi: 10.1126/science.aaa3662.

[2] CDC Centers for Disease Control and Prevention, “Measles Elimination,” Jan. 2022. [Online]. Available: www.cdc.gov/measles/elimination.html

[3] S. Guseva, S. Milles, M. Blackledge, and R. W. H. Ruigrok, “The Nucleoprotein and Phosphoprotein of Measles Virus,” Front. Microbiol., vol. 10, p. 1832, Aug. 2019, doi: 10.3389/fmicb.2019.01832.

[4] J. C. Marie, F. Saltel, J.-M. Escola, P. Jurdic, T. F. Wild, and B. Horvat, “Cell surface delivery of the measles virus nucleoprotein: a viral strategy to induce immunosuppression,” J. Virol., vol. 78, no. 21, pp. 11952–11961, Nov. 2004, doi: 10.1128/JVI.78.21.11952-11961.2004.

[5] K. Ravanel et al., “Measles virus nucleocapsid protein binds to FcgammaRII and inhibits human B cell antibody production,” J. Exp. Med., vol. 186, no. 2, pp. 269–278, Jul. 1997, doi: 10.1084/jem.186.2.269.

[6] J. C. Marie et al., “Mechanism of measles virus-induced suppression of inflammatory immune responses,” Immunity, vol. 14, no. 1, pp. 69–79, Jan. 2001, doi: 10.1016/s1074-7613(01)00090-5.

[7] B. Bankamp, U. G. Brinckmann, A. Reich, S. Niewiesk, V. ter Meulen, and U. G. Liebert, “Measles virus nucleocapsid protein protects rats from encephalitis,” J. Virol., vol. 65, no. 4, pp. 1695–1700, Apr. 1991, doi: 10.1128/JVI.65.4.1695-1700.1991.