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Vaccination mandates for elementary and middle school attendance have been shown to increase vaccination rates and decrease the burden of vaccine-preventable diseases. Fewer studies have evaluated similar requirements for child care attendance. This study provides robust, quasi-experimental estimates of the effect of state laws mandating the pneumococcal conjugate vaccine for child care attendance on vaccination coverage among children aged 19-35 months.Using provider-verified immunization histories from the 2001-2018 waves of the National Immunization Survey-Child and leveraging the staggered implementation of vaccination requirements across states, a generalized difference-in-differences approach was implemented to compare regression-adjusted changes in vaccination coverage among children in states with and without a child care mandate for the pneumococcal conjugate vaccine. The dynamics of estimated treatment effects were analyzed using an event study analysis. All data analyses were conducted in 2019‒2020.State adoption of a child care mandate for the pneumococcal conjugate vaccine increased the likelihood that resident children aged 19-35 months completed the 4-dose pneumococcal conjugate vaccine series by 3.12 percentage points (p0.01). Statistically significant gains in pneumococcal conjugate vaccine coverage were identified in the first year following policy implementation and were found to persist over a period of ≥7 years.Results indicate that state adoption of a child care mandate for the pneumococcal conjugate vaccine leads to an increase in the proportion of resident children aged 19-35 months who are up to date with pneumococcal conjugate vaccine.

Nonmedical exemptions from school-entry vaccine mandates are receiving increased policy and public health scrutiny. This paper examines how expanding the availability of exemptions influences vaccination rates in early childhood and academic achievement in middle school. We leverage 2003 legislation that granted personal belief exemptions (PBE) in Texas and Arkansas, two states that previously allowed exemptions only for medical or religious regions. We find that PBE decreased vaccination coverage among Black and low-income preschoolers by 16.1% and 8.3%, respectively. Furthermore, we find that those cohorts affected by the policy change in early childhood performed less well on standardized tests of academic achievement in middle school. Estimated effects on test scores were largest for Black students and economically disadvantaged students.

To contribute knowledge of the processing and activation of invertebrate proteolytic enzymes, we studied the metalloprotease astacin, a digestive enzyme from the freshwater crayfish Astacus astacus (decapod crustacean). It is the prototype of the protein family of astacins, members of which occur in organisms from bacteria to man and are involved in a variety of physiological reactions. According to its genomic structure, astacin is produced as a zymogen [Geier, G., Jacob, E., Stocker, W. & Zwilling, R. (1997) Arch. Biochem. Biophys.337, 300–307]. To localize and follow the processing of pro-astacin in different parts of the digestive tract, we synthesized two peptides covering the pro part of pro-astacin and raised antibodies against them. In addition, antiserum against the whole active astacin was produced. Using immunohistochemical investigation, we detected pro-astacin in the F cells of the hepatopancreas and all the way into the tubular lumen and the collecting ducts of this gland. Immunoblot assays revealed only active astacin, and never pro-astacin, present in the cardiac stomach. We conclude from these studies that astacin is secreted into the lumen of the hepatopancreatic tubules in its pro form and is activated on its way to the stomach. To investigate which of the two endopeptidases found in the digestive tract of crayfish, astacin or trypsin, is responsible for cleaving the propeptide from pro-astacin, we synthesized different peptides that mimick the activation site. MS analysis of the cleavage products of astacin and trypsin showed that astacin is capable of catalyzing its own activation. Any contribution of trypsin would require the successive action of an aminopeptidase. Substituting glycine for arginine at position −1 of the activation site does not prevent astacin activity. As most members of the astacin protein family have basic amino-acid residues in this position, in these cases also astacin-specific cleavage would be possible.