Institutional trust is a distinct construct related to vaccine hesitancy and refusal.

BACKGROUND: Vaccine hesitancy is driven by a heterogeneous and changing set of psychological, social and historical phenomena, requiring multidisciplinary approaches to its study and intervention. Past research has brought to light instances of both interpersonal and institutional trust playing an important role in vaccine uptake. However, no comprehensive study to date has specifically assessed the relative importance of these two categories of trust as they relate to vaccine behaviors and attitudes. METHODS: In this paper, we examine the relationship between interpersonal and institutional trust and four measures related to COVID-19 vaccine hesitancy and one measure related to general vaccine hesitancy. We hypothesize that, across measures, individuals with vaccine hesitant attitudes and behaviors have lower trust-especially in institutions-than those who are not hesitant. We test this hypothesis in a sample of 1541 Canadians. RESULTS: A deficit in both interpersonal and institutional trust was associated with higher levels of vaccine hesitant attitudes and behaviors. However, institutional trust was significantly lower than interpersonal trust in those with high hesitancy scores, suggesting that the two types of trust can be thought of as distinct constructs in the context of vaccine hesitancy. CONCLUSIONS: Based on our findings, we suggest that diminished institutional trust plays a crucial role in vaccine hesitancy. We propose that this may contribute to a tendency to instead place trust in interpersonally propagated belief systems, which may be more strongly misaligned with mainstream evidence and thus support vaccine hesitancy attitudes. We offer strategies rooted in these observations for creating public health messages designed to enhance vaccine uptake.

Navigating the uncertainty: A novel taxonomy of vaccine hesitancy in the context of COVID-19.

Vaccine hesitancy remains a significant and evolving public health challenge. The COVID-19 pandemic has created a unique decision context with significant uncertainty caused by the novelty of the disease being targeted, unfamiliarity with the vaccines being offered, misinformation, and strong handed government measures. In an effort to extend our understanding of vaccine hesitancy to the high uncertainty decision environment presented by COVID-19, we present a novel taxonomy of the determinants of vaccine hesitancy, based on an inductive analysis of qualitative data gathered during the COVID-19 pandemic. We report on focus group data from a purposive sample of 18 Canadians with varying sociodemographic characteristics and COVID-19 vaccination attitudes. An inductive thematic analysis of this data reveals eight core themes related to vaccine hesitancy: values, trust, social environment, personal anecdotes, environmental fluctuation, prior knowledge, perceived risk & systems of care. We explore these core themes as well as 25 sub-themes, contrasting them with previous models of vaccine hesitancy and suggesting potential strategies for public health professionals.

Inositol phosphate-induced stabilization of inositol 1,3,4,5,6-pentakisphosphate 2-kinase and its role in substrate specificity.

Inositol phosphate kinases (IPKs) sequentially phosphorylate inositol phosphates (IPs) on their inositol rings to yield an array of signaling molecules. IPKs must possess the ability to recognize their physiological substrates from among a pool of over 30 cellular IPs that differ in numbers and positions of phosphates. Crystal structures from IPK subfamilies have revealed structural determinants for IP discrimination, which vary considerably between IPKs. However, recent structures of inositol 1,3,4,5,6-pentakisphosphate 2-kinase (IPK1) did not reveal how IPK1 selectively recognizes its physiological substrate, IP5, while excluding others. Here, we report that limited proteolysis has revealed the presence of multiple conformational states in the IPK1 catalytic cycle, with notable protection from protease only in the presence of IP. Further, a 3.1-Å crystal structure of IPK1 bound to ADP in the absence of IP revealed decreased order in residues 110-140 within the N-lobe of the kinase compared with structures in which IP is bound. Using this solution and crystallographic data, we propose a model for recognition of IP substrate by IPK1 wherein phosphate groups at the 4-, 5-, and 6-positions are recognized initially by the C-lobe with subsequent interaction of the 1-position phosphate by Arg130 that stabilizes this residue and the N-lobe. This model explains how IPK1 can be highly specific for a single IP substrate by linking its interactions with substrate phosphate groups to the stabilization of the N- and C-lobes and kinase activation.