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Imperfect vaccine and hysteresis.

ABSTRACT: Addressing vaccine compliance problems is of particular relevance and significance to public health. Despite resurgence of vaccine-preventable diseases and public awareness of vaccine importance, why is it so challenging to boost population vaccination coverage to desired levels especially in the wake of declining vaccine uptake? To understand this puzzling phenomenon, here we study how social imitation dynamics of vaccination can be impacted by the presence of imperfect vaccine, which only confers partial protection against the disease. Besides weighing the perceived cost of vaccination with the risk of infection, the effectiveness of vaccination is also an important factor driving vaccination decisions. We discover that there can exist multiple stable vaccination equilibria if vaccine efficacy is below a certain threshold. Furthermore, our bifurcation analysis reveals the occurrence of hysteresis loops of vaccination rate with respect to changes in the perceived vaccination cost as well as in the vaccination effectiveness. Moreover, we find that hysteresis is more likely to arise in spatial populations than in well-mixed populations, even for parameter choices that do not allow for bifurcation in the latter. Our work shows that hysteresis can appear as an unprecedented roadblock for the recovery of vaccination uptake, thereby helping explain the persistence of vaccine compliance problem.

SUBMITTER: Chen X

PROVIDER: S-EPMC6367186 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature

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Imperfect vaccine and hysteresis.

Chen Xingru X Fu Feng F

Proceedings. Biological sciences 20190101 1894

Addressing vaccine compliance problems is of particular relevance and significance to public health. Despite resurgence of vaccine-preventable diseases and public awareness of vaccine importance, why is it so challenging to boost population vaccination coverage to desired levels especially in the wake of declining vaccine uptake? To understand this puzzling phenomenon, here we study how social imitation dynamics of vaccination can be impacted by the presence of imperfect vaccine, which only conf ...[more]

PMID: 30963866

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Project description:The three-dimensional structures of macromolecules and their complexes are mainly elucidated by X-ray protein crystallography. A major limitation of this method is access to high-quality crystals, which is necessary to ensure X-ray diffraction extends to sufficiently large scattering angles and hence yields information of sufficiently high resolution with which to solve the crystal structure. The observation that crystals with reduced unit-cell volumes and tighter macromolecular packing often produce higher-resolution Bragg peaks suggests that crystallographic resolution for some macromolecules may be limited not by their heterogeneity, but by a deviation of strict positional ordering of the crystalline lattice. Such displacements of molecules from the ideal lattice give rise to a continuous diffraction pattern that is equal to the incoherent sum of diffraction from rigid individual molecular complexes aligned along several discrete crystallographic orientations and that, consequently, contains more information than Bragg peaks alone. Although such continuous diffraction patterns have long been observed--and are of interest as a source of information about the dynamics of proteins--they have not been used for structure determination. Here we show for crystals of the integral membrane protein complex photosystem II that lattice disorder increases the information content and the resolution of the diffraction pattern well beyond the 4.5-ångström limit of measurable Bragg peaks, which allows us to phase the pattern directly. Using the molecular envelope conventionally determined at 4.5 ångströms as a constraint, we obtain a static image of the photosystem II dimer at a resolution of 3.5 ångströms. This result shows that continuous diffraction can be used to overcome what have long been supposed to be the resolution limits of macromolecular crystallography, using a method that exploits commonly encountered imperfect crystals and enables model-free phasing.

Dataset Information

Imperfect vaccine and hysteresis.

Publications

Imperfect vaccine and hysteresis.

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