Small-angle neutron scattering study of recombinant yeast-derived human hepatitis B virus surface antigen vaccine particle

M. Sato; Y. Ito; K. Kameyama; M. Imai; N. Ishikawa; T. Takagi

doi:10.1016/0921-4526(95)00271-A

Small-angle neutron scattering study of recombinant yeast-derived human hepatitis B virus surface antigen vaccine particle

M. Sato, Y. Ito, K. Kameyama, M. Imai, N. Ishikawa, T. Takagi

SCI - Physics

Research output: Contribution to journal › Article

1 Citation (Scopus)

Abstract

The overall and internal structure of recombinant yeast-derived human hepatitis B virus surface antigen vaccine particles was investigated by small-angle neutron scattering using the contrast variation method. The vaccine is a nearly spherical particle, and its contrast-matching point was determined to be at about 24% D₂O content, indicating that a large part of the vaccine particle is occupied by lipids and carbohydrates from the yeast. The Stuhrmann plot suggests that the surface antigens exist predominantly in the peripheral region of the particle, which is favorable to the induction of anti-virus antibodies.

Original language	English
Pages (from-to)	757-759
Number of pages	3
Journal	Physica B: Physics of Condensed Matter
Volume	213-214
Issue number	C
DOIs	https://doi.org/10.1016/0921-4526(95)00271-A
Publication status	Published - 1995 Aug 1

ASJC Scopus subject areas

Electronic, Optical and Magnetic Materials
Condensed Matter Physics
Electrical and Electronic Engineering

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abstract = "The overall and internal structure of recombinant yeast-derived human hepatitis B virus surface antigen vaccine particles was investigated by small-angle neutron scattering using the contrast variation method. The vaccine is a nearly spherical particle, and its contrast-matching point was determined to be at about 24% D2O content, indicating that a large part of the vaccine particle is occupied by lipids and carbohydrates from the yeast. The Stuhrmann plot suggests that the surface antigens exist predominantly in the peripheral region of the particle, which is favorable to the induction of anti-virus antibodies.",

author = "M. Sato and Y. Ito and K. Kameyama and M. Imai and N. Ishikawa and T. Takagi",

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AU - Sato, M.

AU - Ito, Y.

AU - Kameyama, K.

AU - Imai, M.

AU - Ishikawa, N.

AU - Takagi, T.

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AB - The overall and internal structure of recombinant yeast-derived human hepatitis B virus surface antigen vaccine particles was investigated by small-angle neutron scattering using the contrast variation method. The vaccine is a nearly spherical particle, and its contrast-matching point was determined to be at about 24% D2O content, indicating that a large part of the vaccine particle is occupied by lipids and carbohydrates from the yeast. The Stuhrmann plot suggests that the surface antigens exist predominantly in the peripheral region of the particle, which is favorable to the induction of anti-virus antibodies.

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