Youth Development through Service: A Quality Assessment of the YouthBuild AmeriCorps Program

The YouthBuild AmeriCorps program serves youth facing a multitude of challenges, including a lack of education and job skills, community disengagement, and economic disadvantage. This program assessment found that after engaging with the YouthBuild AmeriCorps model, participants made significant, positive changes in their outlook on service, personal responsibility, and community orientation. More specifically, after participating in the program, they deepened their personal commitments to service, began to develop a sense of personal worth and reliability, became more connected with their communities, and started to develop more trust in larger social institutions. These encouraging findings suggest that YouthBuild AmeriCorps is succeeding in the development of service commitment, a sense of community engagement, and personal satisfaction within students who participate in their construction service, education, and leadership development program

Ready for Success: A Profile of YouthBuild Mentoring Participants

The YouthBuild USA National Mentoring Alliance program (“YouthBuild Mentoring”) seeks to engage students with responsible, supportive, committed adult volunteers to help young people achieve success in education, employment, and social relationships. By matching students with adult mentors for a minimum of 15 months, YouthBuild Mentoring helps these youth form strong emotional bonds and continuing relationships that will ideally last for years beyond the end of the program. YouthBuild USA partnered with the Research and Evaluation Center of John Jay College of Criminal Justice to assess the attitudes of YouthBuild Mentoring participants on a variety of topics, including self-image, self-efficacy, perceptions of social support, family function, attitudes towards society, perceptions of YouthBuild, and education goals. The students reported a high sense of self-efficacy, high self-confidence, and a belief that they can positively impact their communities

Profession loss crisis at an old age: Specific features, factors, and mechanisms of coping

This article discusses the specific characteristics of profession loss crisis at an old age. Profession loss crisis is the last normative crisis of personal professional development that is caused by the completion of one's professional biography after reaching a certain age. The research employs a psychobiographic method and a critical events method. These methods are based on the use of a formalized biographical questionnaire worked out by Norakidze V.G. and reconstructed by Zeer E.F. The authors have identified and provided a detailed description of the main factors that cause profession loss crisis: Random events, adverse circumstances while implementing professional plans, etc. The article outlines the main strategies for coping with this crisis: Changing jobs, re-training, the assistance of colleagues and administration, etc. The authors suggest technologies to minimize the effects of these factors and overcome profession loss crisis effectively. © 2019 by the authors

Durable Collaborations: The National Forum on Youth Violence Prevention

In 2012, the Research and Evaluation Center at John Jay College began to publish the results of an assessment conducted between Summer 2011 and Summer 2012. The project conducted surveys and measured the effectiveness of the National Forum on Youth Violence Prevention. In 2016, with the support of the Office of Juvenile Justice and Delinquency Prevention, the research team tracked perceptions and opinions in each community involved in the National Forum on Youth Violence Prevention

Teaming Up for Safer Cities: A Report from the Implementation Assessment of the National Forum on Youth Violence Prevention (2012)

The efforts inspired by the National Forum on Youth Violence Prevention will take time to develop, but survey results from the first 15 months of implementation suggest that the initiative may be generating some important changes. In five communities, survey respondents report a number of potentially valuable improvements. The results imply that the cities involved in the National Forum may be increasing opportunities for youth and improving the extent to which violence prevention approaches draw upon the perspectives and expertise of a broad range of community members. There are also indications that some cities are developing better overall capacity to reduce youth violence, and local perceptions of law enforcement efficacy may be improving. In 2016, the JohnJayREC research team launched a new iteration of the same survey. To view that report, click here: https://johnjayrec.nyc/2016/06/27/nfyvp2016

Alanine 501 Mutations in Penicillin-Binding Protein 2 from Neisseria gonorrhoeae : Structure, Mechanism, and Effects on Cephalosporin Resistance and Biological Fitness

Resistance of Neisseria gonorrhoeae to expanded-spectrum cephalosporins such as ceftriaxone and cefixime has increased markedly in the past decade. The primary cephalosporin resistance determinant is a mutated penA gene, which encodes the essential peptidoglycan transpeptidase, penicillin-binding protein 2 (PBP2). Decreased susceptibility and resistance can be conferred by mosaic penA alleles containing upward of 60 amino acid changes relative to wild-type PBP2, or by nonmosaic alleles with relatively few mutations, the most important of which occurs at Ala501 located near the active site of PBP2. Recently, fully cefixime- and ceftriaxone-resistant clinical isolates that harbored a mosaic penA allele with an A501P mutation were identified. To examine the potential of mutations at Ala501 to increase resistance to expanded-spectrum cephalosporins, we randomized codon 501 in a mosaic penA allele and transformed N. gonorrhoeae to increased cefixime resistance. Interestingly, only five substitutions of Ala501 (A501V, A501T, A501P, A501R, and A501S) that increased resistance and preserved essential transpeptidase function were isolated. To understand their structural implications, these mutations were introduced into the nonmosaic PBP2-6140CT, which contains four C-terminal mutations present in PBP2 from the penicillin-resistant strain FA6140. The crystal structure of PBP2-6140CT-A501T was determined and revealed ordering of a loop near the active site and a new hydrogen bond involving Thr501 that connects the loop and the SxxK conserved active site motif. The structure suggests that increased rigidity in the active site region is a mechanism for cephalosporin resistance mediated by Ala501 mutations in PBP2

Molecular and Structural Analysis of Mosaic Variants of Penicillin-Binding Protein 2 Conferring Decreased Susceptibility to Expanded-Spectrum Cephalosporins in Neisseria gonorrhoeae : Role of Epistatic Mutations

Mutations in penicillin-binding protein 2 (PBP 2) encoded by mosaic penA alleles are critical for intermediate resistance to the expanded-spectrum cephalosporins ceftriaxone and cefixime in Neisseria gonorrhoeae. Three of the ~60 mutations present in mosaic alleles of penA, G545S, I312M, and V316T, have been reported to be responsible for increased resistance, especially to cefixime (Takahata et al. 2006. Antimicrob Agents Chemother 50:3638-45). However, we observed that the minimum inhibitory concentrations (MICs) of penicillin, ceftriaxone, and cefixime for a wild type strain (FA19) containing a penA gene with these three mutations increased only 1.5-, 1.5-, and 3.5-fold, respectively. In contrast, when these three mutations in a mosaic penA allele (penA35) were reverted back to wild type and the gene transformed into FA19, the MICs of the three antibiotics were reduced to near wild type levels. Thus, these three mutations display epistasis, in that their capacity to increase resistance to β-lactam antibiotics is dependent on the presence of other mutations in the mosaic alleles. We also identified an additional mutation, N512Y, that contributes to decreased susceptibility to expanded-spectrum cephalosporins. Finally, we investigated the effects of a mutation (A501V) currently found only in non-mosaic penA alleles on decreased susceptibility to ceftriaxone and cefixime, under the expectation that this mutation may arise in mosaic alleles. Transfer of the mosaic penA35 allele containing an A501V mutation into FA6140, a chromosomally mediated penicillin-resistant isolate, increased the MICs of ceftriaxone (0.4 μg/ml) and cefixime (1.2μg/ml) to levels above their respective breakpoints. The proposed structural mechanisms of these mutations are discussed in light of the recently published structure of PBP 2

A Highly Conserved Interaction Involving the Middle Residue of the SXN Active-Site Motif Is Crucial for Function of Class B Penicillin-Binding Proteins: Mutational and Computational Analysis of PBP 2 from N. gonorrhoeae

Insertion of an aspartate residue at position 345a in penicillin-binding protein 2 (PBP 2), which lowers the rate of penicillin acylation by ~6-fold, is commonly observed in penicillin-resistant strains of Neisseria gonorrhoeae. Here, we show that insertions of other amino acids also lower the penicillin acylation rate of PBP 2, but none supported growth of N. gonorrhoeae, indicating loss of essential transpeptidase activity. The Asp345a mutation likely acts by altering the interaction between its adjacent residue, Asp346, in the β2a-β2d hairpin loop and Ser363, the middle residue of the SXN active site motif. Because the adjacent aspartate creates ambiguity in the position of the insertion, we also examined if insertions at position 346a could confer decreased susceptibility to penicillin. However, only aspartate insertions were identified, indicating that only an Asp-Asp couple can confer resistance and retain transpeptidase function. The importance of the Asp346-Ser363 interaction was assessed by mutation of each residue to Ala. Although both mutants lowered the acylation rate of penicillin G by 5-fold, neither could support growth of N. gonorrhoeae, again indicating loss of transpeptidase function. Interaction between a residue in the equivalent of the β2a-β2d hairpin loop and the middle residue of the SXN motif is observed in crystal structures of other Class B PBPs and its importance is also supported by multi-sequence alignments. Overall, these results suggest that this conserved interaction can be manipulated (e.g. by insertion) to lower the acylation rate by β-lactam antibiotics and increase resistance, but only if essential transpeptidase activity is preserved

Identification of Amino Acids Conferring High-Level Resistance to Expanded-Spectrum Cephalosporins in the penA Gene from Neisseria gonorrhoeae Strain H041

ABSTRACT The recent identification of a high-level-ceftriaxone-resistant (MIC = 2 to 4 μg/ml) isolate of Neisseria gonorrhoeae from Japan (H041) portends the loss of ceftriaxone as an effective treatment for gonococcal infections. This is of grave concern because ceftriaxone is the last remaining option for first-line empirical antimicrobial monotherapy. The penA gene from H041 ( penA41 ) is a mosaic penA allele similar to mosaic alleles conferring intermediate-level cephalosporin resistance (Ceph i ) worldwide but has 13 additional mutations compared to the mosaic penA gene from the previously studied Ceph i strain 35/02 ( penA35 ). When transformed into the wild-type strain FA19, the penA41 allele confers 300- and 570-fold increases in the MICs for ceftriaxone and cefixime, respectively. In order to understand the mechanisms involved in high-level ceftriaxone resistance and to improve surveillance and epidemiology during the potential emergence of ceftriaxone resistance, we sought to identify the minimum number of amino acid alterations above those in penA35 that confer high-level resistance to ceftriaxone. Using restriction fragment exchange and site-directed mutagenesis, we identified three mutations, A311V, T316P, and T483S, that, when incorporated into the mosaic penA35 allele, confer essentially all of the increased resistance of penA41 . A311V and T316P are close to the active-site nucleophile Ser310 that forms the acyl-enzyme complex, while Thr483 is predicted to interact with the carboxylate of the β-lactam antibiotic. These three mutations have thus far been described only for penA41 , but dissemination of these mutations in other mosaic alleles would spell the end of ceftriaxone as an effective treatment for gonococcal infections