Dialek dan Campur Kode Ujaran Bahasa Masyarakat Desa Pulau Belimbing Kabupaten Kampar

The main human communication tool is language which is used as an exchange of information between people, be it arguments, ideas or feelings. The use of language in people's daily lives can affect articulation in communicating and interacting between humans. Diversity in language creates its own uniqueness in communicating. The use of the language of the people in the tourist village of Belimbing Island is greatly influenced by the environment. This is what causes the mixed dialect used by the Belimbing Island villagers to be very unique and diverse. The purpose of this research is to know and study the diversity of languages ​​used by the people in the tourist village of Belimbing Island and to describe the Dialect and Code Mixing of the speech of the people in Wista Village, Belimbing Island. The method used is descriptive qualitative and sociolinguistic approach. The results of the study indicate the use of dialect and code mixing in communication carried out by the people in the tourist village of Belimbing Island

Pemanfaatan Desa Wisata Pulau Belimbing Sebagai Sumber Pembelajaran Bahasa Indonesia Berbasis Kearifan Lokal

Desa Wisata Pulau Belimbing menjadi salah satu bukti kekayaan budaya yang dimiliki oleh Indonesia. Sampai saat ini masih dapat dinikmati dan selalu diupayakan pelestariannya. Banyak objek wisata berbau budaya yang dapat dinikmati di desa ini. Desa ini memiliki pesona kebudayaan yang sangat menyentuh, yaitu sebuah desa tua yang masih asri dan terdapat banyak rumah-rumah tua yang sudah berusia ratusan tahun. Rumah Lontiok adalah salah satu rumah adat yang tetap dijaga hingga sekarang. Rumah adat ini sudah diresmikan pada tahun 2007 sebagai rumah adat Kabupaten Kampar. Di bagian belakang rumah lontiok terdapat gelek tobu atau penggiling tebu. Pada zaman dahulu gelek tobu ini digunakan untuk menggelek tebu dan yang kemudian dimasak dan dijadikan manisan atau gula tebu. Selanjutnya ada calempong dan silat persembahan yang merupakan tradisi masyarakat Desa Wisata Pulau Belimbing dalam menyambut tamu. Selanjutnya salah satu permainna rakyat yang masih ada hingga saat ini ialah permainan engrang. Segala kebudayaan yang ada di Desa Wisata Pulau Belimbing ini dapat diintegrasikan ke dalam pembelajaran, baik secara langsung maupun tidak langsung. Peserta didik akan merasa memiliki kebudayaannya sendiri dan secara tidak langsung karakter atau jati diri asli dari masyarakat Indonesia akan tertanam di dalam diri peserta didik. Penelitian ini menggunakan jenis penelitia etnografi. Teknik pengumpulan data ialah dengan observasi secara langsung, wawancara, dan domunentasi untuk mengetahui kearifan lokal masyarakat Desa Wisata Pulau Belimbing. Hasil dari penelitian inilah yang nantinya dapat diintegrasikan ke dalam pembelajaran kemudian dapat diimplementasikan dengan harapan agar tujuan pembelajaran dapat dicapai dengan maksimal

A Receptor-based Switch that Regulates Anthrax Toxin Pore Formation

Cellular receptors can act as molecular switches, regulating the sensitivity of microbial proteins to conformational changes that promote cellular entry. The activities of these receptor-based switches are only partially understood. In this paper, we sought to understand the mechanism that underlies the activity of the ANTXR2 anthrax toxin receptor-based switch that binds to domains 2 and 4 of the protective antigen (PA) toxin subunit. Receptor-binding restricts structural changes within the heptameric PA prepore that are required for pore conversion to an acidic endosomal compartment. The transfer cross-saturation (TCS) NMR approach was used to monitor changes in the heptameric PA-receptor contacts at different steps during prepore-to-pore conversion. These studies demonstrated that receptor contact with PA domain 2 is weakened prior to pore conversion, defining a novel intermediate in this pathway. Importantly, ANTXR2 remained bound to PA domain 4 following pore conversion, suggesting that the bound receptor might influence the structure and/or function of the newly formed pore. These studies provide new insights into the function of a receptor-based molecular switch that controls anthrax toxin entry into cells

Diverse structural approaches to haem appropriation by pathogenic bacteria

The critical need for iron presents a challenge for pathogenic bacteria that must survive in an environment bereft of accessible iron due to a natural low bioavailability and their host's nutritional immunity. Appropriating haem, either direct from host haemoproteins or by secreting haem-scavenging haemophores, is one way pathogenic bacteria can overcome this challenge. After capturing their target, haem appropriation systems must remove haem from a high-affinity binding site (on the host haemoprotein or bacterial haemophore) and transfer it to a binding site of lower affinity on a bacterial receptor. Structural information is now available to show how, using a combination of induced structural changes and steric clashes, bacteria are able to extract haem from haemophores, haemopexin and haemoglobin. This review focuses on structural descriptions of these bacterial haem acquisition systems, summarising how they bind haem and their target haemoproteins with particularly emphasis on the mechanism of haem extraction

Delayed Toxicity Associated with Soluble Anthrax Toxin Receptor Decoy-Ig Fusion Protein Treatment

Soluble receptor decoy inhibitors, including receptor-immunogloubulin (Ig) fusion proteins, have shown promise as candidate anthrax toxin therapeutics. These agents act by binding to the receptor-interaction site on the protective antigen (PA) toxin subunit, thereby blocking toxin binding to cell surface receptors. Here we have made the surprising observation that co-administration of receptor decoy-Ig fusion proteins significantly delayed, but did not protect, rats challenged with anthrax lethal toxin. The delayed toxicity was associated with the in vivo assembly of a long-lived complex comprised of anthrax lethal toxin and the receptor decoy-Ig inhibitor. Intoxication in this system presumably results from the slow dissociation of the toxin complex from the inhibitor following their prolonged circulation. We conclude that while receptor decoy-Ig proteins represent promising candidates for the early treatment of B. anthracis infection, they may not be suitable for therapeutic use at later stages when fatal levels of toxin have already accumulated in the bloodstream

Differential Function of Lip Residues in the Mechanism and Biology of an Anthrax Hemophore

To replicate in mammalian hosts, bacterial pathogens must acquire iron. The majority of iron is coordinated to the protoporphyrin ring of heme, which is further bound to hemoglobin. Pathogenic bacteria utilize secreted hemophores to acquire heme from heme sources such as hemoglobin. Bacillus anthracis, the causative agent of anthrax disease, secretes two hemophores, IsdX1 and IsdX2, to acquire heme from host hemoglobin and enhance bacterial replication in iron-starved environments. Both proteins contain NEAr-iron Transporter (NEAT) domains, a conserved protein module that functions in heme acquisition in Gram-positive pathogens. Here, we report the structure of IsdX1, the first of a Gram-positive hemophore, with and without bound heme. Overall, IsdX1 forms an immunoglobin-like fold that contains, similar to other NEAT proteins, a 310-helix near the heme-binding site. Because the mechanistic function of this helix in NEAT proteins is not yet defined, we focused on the contribution of this region to hemophore and NEAT protein activity, both biochemically and biologically in cultured cells. Site-directed mutagenesis of amino acids in and adjacent to the helix identified residues important for heme and hemoglobin association, with some mutations affecting both properties and other mutations affecting only heme stabilization. IsdX1 with mutations that reduced the ability to associate with hemoglobin and bind heme failed to restore the growth of a hemophore-deficient strain of B. anthracis on hemoglobin as the sole iron source. These data indicate that not only is the 310-helix important for NEAT protein biology, but also that the processes of hemoglobin and heme binding can be both separate as well as coupled, the latter function being necessary for maximal heme-scavenging activity. These studies enhance our understanding of NEAT domain and hemophore function and set the stage for structure-based inhibitor design to block NEAT domain interaction with upstream ligands

IlsA, A Unique Surface Protein of Bacillus cereus Required for Iron Acquisition from Heme, Hemoglobin and Ferritin

The human opportunistic pathogen Bacillus cereus belongs to the B. cereus group that includes bacteria with a broad host spectrum. The ability of these bacteria to colonize diverse hosts is reliant on the presence of adaptation factors. Previously, an IVET strategy led to the identification of a novel B. cereus protein (IlsA, Iron-regulated leucine rich surface protein), which is specifically expressed in the insect host or under iron restrictive conditions in vitro. Here, we show that IlsA is localized on the surface of B. cereus and hence has the potential to interact with host proteins. We report that B. cereus uses hemoglobin, heme and ferritin, but not transferrin and lactoferrin. In addition, affinity tests revealed that IlsA interacts with both hemoglobin and ferritin. Furthermore, IlsA directly binds heme probably through the NEAT domain. Inactivation of ilsA drastically decreases the ability of B. cereus to grow in the presence of hemoglobin, heme and ferritin, indicating that IlsA is essential for iron acquisition from these iron sources. In addition, the ilsA mutant displays a reduction in growth and virulence in an insect model. Hence, our results indicate that IlsA is a key factor within a new iron acquisition system, playing an important role in the general virulence strategy adapted by B. cereus to colonize susceptible hosts

Acoustic-induced drag on a bubble

This work reports experiments that show that the drag on a bubble can be modified by the presence of isotropic, homogeneous broadband acoustic noise, when the band overlaps the bubble's resonance width. This constitutes an acoustic analog to the Einstein-Hopf drag on an electromagnetic dipole oscillator in the presence of isotropic and homogeneous electromagnetic fluctuations. In contrast with the electromagnetic Einstein-Hopf drag, band- limited acoustic noise can reduce the drag when the lower frequency of the spectrum coincides with the resonant frequency of the bubble. The modification of the drag experienced by a bubble in the presence of acoustic noise suggests possible applications to bubble migration and to heat transfer in a two-phase fluid. Depending on its size (i.e., resonant frequency), a bubble will experience less or more drag when the fluid is insonified with broadband noise, thereby modifying and possibly controlling bubble migration and heat transfer.http://archive.org/details/acousticinducedd1094513588U.S. Navy (U.S.N.) author.Approved for public release; distribution is unlimited

Molecular mechanisms of bio-catalysis of heme extraction from hemoglobin

Red blood cell hemolysis in sickle cell disease (SCD) releases free hemoglobin. Extracellular hemoglobin and its degradation products, free heme and iron, are highly toxic due to oxidative stress induction and decrease in nitric oxide availability. We propose an approach that helps to eliminate extracellular hemoglobin toxicity in SCD by employing a bacterial protein system that evolved to extract heme from extracellular hemoglobin. NEAr heme Transporter (NEAT) domains from iron-regulated surface determinant proteins from Staphylococcus aureus specifically bind free heme as well as facilitate its extraction from hemoglobin. We demonstrate that a purified NEAT domain fused with human haptoglobin β-chain is able to remove heme from hemoglobin and reduce heme content and peroxidase activity of hemoglobin. We further use molecular dynamics (MD) simulations to resolve molecular pathway of heme transfer from hemoglobin to NEAT, and to elucidate molecular mechanism of such heme transferring process. Our study is the first of its kind, in which simulations are employed to characterize the process of heme leaving hemoglobin and subsequent rebinding with a NEAT domain. Our MD results highlight important amino acid residues that facilitate heme transfer and will guide further studies for the selection of best NEAT candidate to attenuate free hemoglobin toxicity. Keywords: Sickle cell disease, Heme scavenger, Molecular dynamics simulations, Heme-protein binding modelin