<?xml version="1.0" encoding="UTF-8"?>
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<title>Artikel in Fachzeitschriften</title>
<link href="http://edoc.rki.de/176904/43" rel="alternate"/>
<subtitle/>
<id>http://edoc.rki.de/176904/43</id>
<updated>2026-09-20T12:03:40Z</updated>
<dc:date>2026-09-20T12:03:40Z</dc:date>
<entry>
<title>Stellungnahme der STIKO zur Bedeutung der Influenza-Impfempfehlung für Kinder und Jugendliche mit erhöhter gesundheitlicher Gefährdung</title>
<link href="http://edoc.rki.de/176904/13928" rel="alternate"/>
<author>
<name>Ständige Impfkommission (STIKO) beim Robert Koch-Institut</name>
</author>
<id>http://edoc.rki.de/176904/13928</id>
<updated>2026-09-17T12:27:27Z</updated>
<published>2026-09-17T00:00:00Z</published>
<summary type="text">Stellungnahme der STIKO zur Bedeutung der Influenza-Impfempfehlung für Kinder und Jugendliche mit erhöhter gesundheitlicher Gefährdung
Ständige Impfkommission (STIKO) beim Robert Koch-Institut
Stellungnahme der STIKO zur Bedeutung der Influenza-Impfempfehlung für Kinder und Jugendliche mit erhöhter gesundheitlicher Gefährdung&#13;
Die Ständige Impfkommission (STIKO) empfiehlt eindringlich, der bestehenden Influenza-Impfempfehlung nachzukommen und Kinder und Jugendliche mit Risikofaktoren durch eine rechtzeitige Impfung zu schützen. In dieser Stellungnahme geht die STIKO auf die bestehende Indikationsimpfempfehlung für Kinder und Jugendliche sowie auf die verfügbaren Influenza-Impfstoffe ein und verdeutlicht deren Bedeutung anhand von Daten zu Influenza-bedingten Hospitalisierungen bei Kindern und Jugendlichen mit Grunderkrankungen.; English&#13;
Statement by the STIKO on the importance of the influenza vaccination recommendation for children and adolescents at increased health risk&#13;
The Standing Committee on Vaccination (STIKO) strongly urges adherence to the existing influenza vaccination recommendation and calls for children and adolescents with risk factors to be protected through timely vaccination. In this statement, the STIKO addresses the current vaccination recommendation for children and adolescents, as well as the available influenza vaccines, and highlights their importance using data on influenza-related hospitalisations among children and adolescents with medical preconditions.
</summary>
<dc:date>2026-09-17T00:00:00Z</dc:date>
</entry>
<entry>
<title>Influenza-Impfquoten bei Kindern und Jugendlichen mit Grunderkrankung in Deutschland</title>
<link href="http://edoc.rki.de/176904/13927" rel="alternate"/>
<author>
<name>Steffen, Annika</name>
</author>
<author>
<name>Rieck, Thorsten</name>
</author>
<author>
<name>Lottes, Matthäus</name>
</author>
<author>
<name>Rau, Cornelius</name>
</author>
<id>http://edoc.rki.de/176904/13927</id>
<updated>2026-09-17T12:27:26Z</updated>
<published>2026-09-17T00:00:00Z</published>
<summary type="text">Influenza-Impfquoten bei Kindern und Jugendlichen mit Grunderkrankung in Deutschland
Steffen, Annika; Rieck, Thorsten; Lottes, Matthäus; Rau, Cornelius
Seit mehr als 30 Jahren besteht die Empfehlung der Ständigen Impfkommission (STIKO), Kinder und Jugendliche mit bestimmten Grunderkrankungen jährlich gegen Grippe (Influenza) zu impfen. Dennoch waren laut einer Auswertung von Abrechnungsdaten der Kassenärztlichen Vereinigungen (KV) über einen Zeitraum von 11 Saisons (2014/15 bis 2024/25) nur etwa 10 % der Kinder und Jugendlichen mit impfrelevanter Grunderkrankung in der jeweiligen Influenza-Saison gegen Influenza geimpft. Bei unveränderter Impfquote hätten damit auch in der Saison 2026/27 etwa 1,1 Mio. Kinder und Jugendliche mit Grunderkrankung keinen Influenza-Impfschutz.; Influenza immunisation coverage among children and adolescents with medical preconditions in Germany&#13;
For more than 30 years, the Standing Committee on Vaccination (STIKO) has recommended that children and adolescents with certain medical preconditions receive an annual flu (influenza) vaccination. Nevertheless, according to an analysis of data from the Associations of Statutory Health Insurance Physicians (ASHIP) covering a period of 11 seasons (2014/15 to 2024/25), only around 10 % of children and adolescents with a medical precondition for which vaccination is recommended were vaccinated against influenza during the respective influenza season. If the vaccination rate remains unchanged, this would mean that, in the 2026/27 season, around 1.1 million children and adolescents with medical preconditions will have no protection against influenza.
</summary>
<dc:date>2026-09-17T00:00:00Z</dc:date>
</entry>
<entry>
<title>A Plasmodium cysteine protease required for efficient transition from the liver infection stage</title>
<link href="http://edoc.rki.de/176904/13925" rel="alternate"/>
<author>
<name>Putrianti, Elyzana Dewi</name>
</author>
<author>
<name>Schmidt-Christensen, Anja</name>
</author>
<author>
<name>Heussler, Volker</name>
</author>
<author>
<name>Matuschewski, Kai</name>
</author>
<author>
<name>Ingmundson, Alyssa</name>
</author>
<id>http://edoc.rki.de/176904/13925</id>
<updated>2026-09-15T15:27:28Z</updated>
<published>2020-09-21T00:00:00Z</published>
<summary type="text">A Plasmodium cysteine protease required for efficient transition from the liver infection stage
Putrianti, Elyzana Dewi; Schmidt-Christensen, Anja; Heussler, Volker; Matuschewski, Kai; Ingmundson, Alyssa
The transitions between developmental stages are critical points in the Plasmodium life cycle. The development of Plasmodium in the livers of their mammalian hosts bridges malaria transmission and the onset of clinical symptoms elicited by red blood cell infection. The egress of Plasmodium parasites from the liver must be a carefully orchestrated process to ensure a successful switch to the blood stage of infection. Cysteine protease activity is known to be required for liver-stage Plasmodium egress, but the crucial cysteine protease(s) remained unidentified. Here, we characterize a member of the papain-like cysteine protease family, Plasmodium berghei serine repeat antigen 4 (PbSERA4), that is required for efficient initiation of blood-stage infection. Through the generation PbSERA4-specific antisera and the creation of transgenic parasites expressing fluorescently tagged protein, we show that PbSERA4 is expressed and proteolytically processed in the liver and blood stages of infection. Targeted disruption of PbSERA4 results in viable and virulent blood-stage parasites. However, upon transmission from mosquitoes to mice, Pbsera4(-) parasites displayed a reduced capacity to initiate a new round of asexual blood-stage replication. Our results from cultured cells indicate that this defect results from an inability of the PbSERA4-deficient parasites to egress efficiently from infected cells at the culmination of liver-stage development. Protection against infection with wildtype P. berghei could be generated in animals in which Pbsera4(-) parasites failed to establish infection. Our findings confirm that liver-stage merozoite release is an active process and demonstrate that this parasite-encoded cysteine protease contributes to parasite escape from the liver.; Plasmodium parasites cause over 200 million cases of malaria every year. When parasites are transmitted by mosquito bite, they initially colonize the liver before they move into the blood and cause disease. During successful transition from the liver into the blood, Plasmodium cloak themselves in host plasma membrane as they egress from the liver cells. Although some aspects of how Plasmodium exit their host hepatocytes appear unique, certain attributes are shared across diverse pathogens. For example, protease activity is required not only for multiple stages of Plasmodium exit, but is also involved in the egress of some bacteria and other protozoan. Here we characterize a protease in Plasmodium berghei that is expressed in the liver and conserved across Plasmodium species. Through gene targeting, we found PbSERA4 is required for efficient egress of Plasmodium from the liver. In the absence of this protease the transition between the liver and blood stages of growth is prolonged due to inefficient parasite release from liver cells. These findings provide new insights into the function of a conserved Plasmodium protease and into the process of Plasmodium escape from the liver.
</summary>
<dc:date>2020-09-21T00:00:00Z</dc:date>
</entry>
<entry>
<title>Local c-di-GMP Signaling in the Control of Synthesis of the E. coli Biofilm Exopolysaccharide pEtN-Cellulose</title>
<link href="http://edoc.rki.de/176904/13924" rel="alternate"/>
<author>
<name>Richter, Anja M.</name>
</author>
<author>
<name>Possling, Alexandra</name>
</author>
<author>
<name>Malysheva, Nadezhda</name>
</author>
<author>
<name>Yousef, Kaveh P.</name>
</author>
<author>
<name>Herbst, Susanne</name>
</author>
<author>
<name>von Kleist, Max</name>
</author>
<author>
<name>Hengge, Regine</name>
</author>
<id>http://edoc.rki.de/176904/13924</id>
<updated>2026-09-15T14:57:27Z</updated>
<published>2020-07-24T00:00:00Z</published>
<summary type="text">Local c-di-GMP Signaling in the Control of Synthesis of the E. coli Biofilm Exopolysaccharide pEtN-Cellulose
Richter, Anja M.; Possling, Alexandra; Malysheva, Nadezhda; Yousef, Kaveh P.; Herbst, Susanne; von Kleist, Max; Hengge, Regine
In many bacteria, the biofilm-promoting second messenger c-di-GMP is produced and degraded by multiple diguanylate cyclases (DGC) and phosphodiesterases (PDE), respectively. High target specificity of some of these enzymes has led to theoretical concepts of “local” c-di-GMP signaling. In Escherichia coli K-12, which has 12 DGCs and 13 PDEs, a single DGC, DgcC, is specifically required for the biosynthesis of the biofilm exopolysaccharide pEtN-cellulose without affecting the cellular c-di-GMP pool, but the mechanistic basis of this target specificity has remained obscure. DGC activity of membrane-associated DgcC, which is demonstrated in vitro in nanodiscs, is shown to be necessary and sufficient to specifically activate cellulose biosynthesis in vivo. DgcC and a particular PDE, PdeK (encoded right next to the cellulose operon), directly interact with cellulose synthase subunit BcsB and with each other, thus establishing physical proximity between cellulose synthase and a local source and sink of c-di-GMP. This arrangement provides a localized, yet open source of c-di-GMP right next to cellulose synthase subunit BcsA, which needs allosteric activation by c-di-GMP. Through mathematical modeling and simulation, we demonstrate that BcsA binding from the low cytosolic c-di-GMP pool in E. coli is negligible, whereas a single c-di-GMP molecule that is produced and released in direct proximity to cellulose synthase increases the probability of c-di-GMP binding to BcsA several hundred-fold. This local c-di-GMP signaling could provide a blueprint for target-specific second messenger signaling also in other bacteria where multiple second messenger producing and degrading enzymes exist.
</summary>
<dc:date>2020-07-24T00:00:00Z</dc:date>
</entry>
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