Anti-HSPA9 Monoclonal Antibody, Clone 0G9 (DCABH-5563) This Product Is for Research Use Only and Is Not Intended for Diagnostic Use

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Anti-HSPA9 monoclonal antibody, clone 0G9 (DCABH-5563) This product is for research use only and is not intended for diagnostic use. PRODUCT INFORMATION Product Overview Mouse monoclonal to Grp75 Antigen Description Implicated in the control of cell proliferation and cellular aging. May also act as a chaperone. Immunogen Recombinant full length protein corresponding to Human Grp75. Expressed in 293T cells.Database link: Q8N1C8 Isotype IgG Source/Host Mouse Species Reactivity Rat, Human, Primates Clone 0G9 Purity Protein A purified Conjugate Unconjugated Applications WB, ICC/IF, IP Positive Control 293T, HeLa, K562, A431, COS7 and NRK lysates; HeLa cells. Format Liquid Size 100 μg Buffer Preservative: 0.05% Sodium azide; Constituents: 0.1% BSA, 30% Glycerol, 69% PBS Preservative 0.05% Sodium Azide Storage Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle. Ship Shipped at 4°C. GENE INFORMATION Gene Name HSPA9 heat shock 70kDa protein 9 (mortalin) [ Homo sapiens ] 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 1 © Creative Diagnostics All Rights Reserved Official Symbol HSPA9 Synonyms HSPA9; heat shock 70kDa protein 9 (mortalin); heat shock 70kDa protein 9B (mortalin 2) , HSPA9B; stress-70 protein, mitochondrial; GRP75; mot 2; mthsp75; PBP74; mortalin-2; p66- mortalin; mortalin, perinuclear; heat shock 70kD protein 9B; peptide-binding p Entrez Gene ID 3313 Protein Refseq NP_004125 UniProt ID P38646 Chromosome Location 5q31.1 Pathway Metabolism of proteins, organism-specific biosystem; Mitochondrial Protein Import, organism- specific biosystem; RNA degradation, organism-specific biosystem; RNA degradation, conserved biosystem; Tuberculosis, organism-specific biosystem; Tuberculosis, conserved biosystem; Function ATP binding; enzyme binding; nucleotide binding; protein binding; unfolded protein binding; 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 2 © Creative Diagnostics All Rights Reserved.

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Anti-HSPA9 Antibody
FOR RESEARCH USE ONLY! 09/19 Anti-HSPA9 Antibody CATALOG NO.: A1861-100 100 µl. BACKGROUND DESCRIPTION: This gene encodes a member of the heat shock protein 70 gene family. The encoded protein is primarily localized to the mitochondria but is also found in the endoplasmic reticulum, plasma membrane and cytoplasmic vesicles. This protein is a heat-shock cognate protein. This protein plays a role in cell proliferation, stress response and maintenance of the mitochondria. A pseudogene of this gene is found on chromosome 2. ALTERNATE NAMES: CSA, PBP74, MOT, MTHSP75, SAAN, HSPA9, HSPA9B, SIDBA4, mitochondrial, EVPLS, CRP40 . ANTIBODY TYPE: Polyclonal HOST/ISOTYPE: Rabbit / Rabbit IgG. IMMUNOGEN: Recombinant fusion protein containing a sequence corresponding to amino acids 380-679 of human HSPA9 (NP_004125.3). PURIFICATION: Affinity purification. FORM: Liquid. FORMULATION: Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3. SPECIES REACTIVITY: Rat. Mouse. Human. STORAGE CONDITIONS: Store at -20°C; Avoid freeze / thaw cycles. APPLICATIONS AND USAGE: IF 1:50 - 1:200. WB 1:500 - 1:2000. IHC 1:50 - 1:200. Immunofluorescence analysis of U2OS cells using HSPA9 antibody. Blue: DAPI for nuclear staining.. Immunohistochemistry of paraffin-embedded rat kidney using HSPA9 antibody at dilution of 1:100. 155 S. Milpitas Blvd., Milpitas, CA 95035 USA | T: (408)493-1800 F: (408)493-1801 | www.biovision.com | [email protected] FOR RESEARCH USE ONLY! Immunohistochemistry of paraffin-embedded human lung cancer using HSPA9 antibody at dilution of 1:100 Immunohistochemistry of paraffin-embedded mouse heart using HSPA9 antibody at dilution of 1:100 Immunohistochemistry of paraffin-embedded human gastric cancer using HSPA9 antibody at dilution of 1:100 Western blot analysis of extracts of various cell lines, using HSPA9 antibody at 1:1000 dilution.
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Deregulated Gene Expression Pathways in Myelodysplastic Syndrome Hematopoietic Stem Cells
Leukemia (2010) 24, 756–764 & 2010 Macmillan Publishers Limited All rights reserved 0887-6924/10 $32.00 www.nature.com/leu ORIGINAL ARTICLE Deregulated gene expression pathways in myelodysplastic syndrome hematopoietic stem cells A Pellagatti1, M Cazzola2, A Giagounidis3, J Perry1, L Malcovati2, MG Della Porta2,MJa¨dersten4, S Killick5, A Verma6, CJ Norbury7, E Hellstro¨m-Lindberg4, JS Wainscoat1 and J Boultwood1 1LRF Molecular Haematology Unit, NDCLS, John Radcliffe Hospital, Oxford, UK; 2Department of Hematology Oncology, University of Pavia Medical School, Fondazione IRCCS Policlinico San Matteo, Pavia, Italy; 3Medizinische Klinik II, St Johannes Hospital, Duisburg, Germany; 4Division of Hematology, Department of Medicine, Karolinska Institutet, Stockholm, Sweden; 5Department of Haematology, Royal Bournemouth Hospital, Bournemouth, UK; 6Albert Einstein College of Medicine, Bronx, NY, USA and 7Sir William Dunn School of Pathology, University of Oxford, Oxford, UK To gain insight into the molecular pathogenesis of the the World Health Organization.6,7 Patients with refractory myelodysplastic syndromes (MDS), we performed global gene anemia (RA) with or without ringed sideroblasts, according to expression profiling and pathway analysis on the hemato- poietic stem cells (HSC) of 183 MDS patients as compared with the the French–American–British classification, were subdivided HSC of 17 healthy controls. The most significantly deregulated based on the presence or absence of multilineage dysplasia. In pathways in MDS include interferon signaling, thrombopoietin addition, patients with RA with excess blasts (RAEB) were signaling and the Wnt pathways. Among the most signifi- subdivided into two categories, RAEB1 and RAEB2, based on the cantly deregulated gene pathways in early MDS are immuno- percentage of bone marrow blasts.
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Stress-Responsive Regulation of Mitochondria Through the ER
TEM-969; No. of Pages 10 Review Stress-responsive regulation of mitochondria through the ER unfolded protein response T. Kelly Rainbolt, Jaclyn M. Saunders, and R. Luke Wiseman Department of Molecular and Experimental Medicine, Department of Chemical Physiology, The Scripps Research Institute, La Jolla, CA 92037, USA The endoplasmic reticulum (ER) and mitochondria form function is sensitive to pathologic insults that induce ER physical interactions involved in the regulation of bio- stress (defined by the increased accumulation of misfolded logic functions including mitochondrial bioenergetics proteins within the ER lumen). ER stress can be transmit- and apoptotic signaling. To coordinate these functions ted to mitochondria by alterations in the transfer of me- 2+ during stress, cells must coregulate ER and mitochon- tabolites such as Ca or by stress-responsive signaling dria through stress-responsive signaling pathways such pathways, directly influencing mitochondrial functions. as the ER unfolded protein response (UPR). Although the Depending on the extent of cellular stress, the stress UPR is traditionally viewed as a signaling pathway re- signaling from the ER to mitochondria can result in pro- sponsible for regulating ER proteostasis, it is becoming survival or proapoptotic adaptations in mitochondrial increasingly clear that the protein kinase RNA (PKR)-like function. endoplasmic reticulum kinase (PERK) signaling pathway During the early adaptive phase of ER stress, ER– 2+ within the UPR can also regulate mitochondria proteos- mitochondrial contacts increase, promoting Ca transfer 2+ tasis and function in response to pathologic insults that between these organelles [4]. This increase in Ca flux into induce ER stress. Here, we discuss the contributions of mitochondria stimulates mitochondrial metabolism 2+ PERK in coordinating ER–mitochondrial activities and through the activity of Ca -regulated dehydrogenases describe the mechanisms by which PERK adapts mito- involved in the tricarboxylic acid (TCA) cycle.
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A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated.
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Allosteric HSP70 Inhibitors Perturb Mitochondrial Proteostasis and Overcome Proteasome Inhibitor Resistance in Multiple Myeloma
bioRxiv preprint doi: https://doi.org/10.1101/2020.04.21.052456; this version posted April 23, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Title: Allosteric HSP70 inhibitors perturb mitochondrial proteostasis and overcome proteasome inhibitor resistance in multiple myeloma Authors: Ian D. Ferguson1, Yu-Hsiu T. Lin1,+, Christine Lam1,+, Hao Shao2, Martina Hale1, Kevin M. Tharp3, Margarette C. Mariano1, Veronica Steri4, Donghui Wang4, Paul Phojanokong4, Sami T. Tuomivaara1, Byron Hann4, Christoph Driessen5, Brian Van Ness6, Jason E. Gestwicki2, Arun P. Wiita1,* Affiliations: 1Dept. of Laboratory Medicine, 2Institute for Neurodegenerative Disease, 3Dept. of Surgery, 4Helen Diller Family Comprehensive Cancer Center, University of California, San Francisco, CA, USA, 5Department of Oncology and Hematology, Kantonsspital St. Gallen, St. Gallen, Switzerland, 6Department of Genetics, Cell Biology & Development, University of Minnesota, Minneapolis, MN, USA. +equal contribution. *Correspondence: Arun P. Wiita, MD, PhD UCSF Dept. of Laboratory Medicine [email protected] 1 bioRxiv preprint doi: https://doi.org/10.1101/2020.04.21.052456; this version posted April 23, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Abstract Proteasome inhibitor (PI) resistance remains a central challenge in multiple myeloma. To identify pathways mediating resistance, we first map proteasome-associated genetic co- dependencies. We identify cytosolic heat shock protein 70 (HSP70) chaperones as potential targets, consistent with proposed mechanisms of myeloma tumor cells overcoming PI-induced stress. These results lead us to explore allosteric HSP70 inhibitors (JG compounds) as myeloma therapeutics.
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At Elevated Temperatures, Heat Shock Protein Genes Show Altered Ratios Of
EXPERIMENTAL AND THERAPEUTIC MEDICINE 22: 900, 2021 At elevated temperatures, heat shock protein genes show altered ratios of different RNAs and expression of new RNAs, including several novel HSPB1 mRNAs encoding HSP27 protein isoforms XIA GAO1,2, KEYIN ZHANG1,2, HAIYAN ZHOU3, LUCAS ZELLMER4, CHENGFU YUAN5, HAI HUANG6 and DEZHONG JOSHUA LIAO2,6 1Department of Pathology, Guizhou Medical University Hospital; 2Key Lab of Endemic and Ethnic Diseases of The Ministry of Education of China in Guizhou Medical University; 3Clinical Research Center, Guizhou Medical University Hospital, Guiyang, Guizhou 550004, P.R. China; 4Masonic Cancer Center, University of Minnesota, Minneapolis, MN 55455, USA; 5Department of Biochemistry, China Three Gorges University, Yichang, Hubei 443002; 6Center for Clinical Laboratories, Guizhou Medical University Hospital, Guiyang, Guizhou 550004, P.R. China Received December 16, 2020; Accepted May 10, 2021 DOI: 10.3892/etm.2021.10332 Abstract. Heat shock proteins (HSP) serve as chaperones genes may engender multiple protein isoforms. These results to maintain the physiological conformation and function of collectively suggested that, besides increasing their expres‑ numerous cellular proteins when the ambient temperature is sion, certain HSP and associated genes also use alternative increased. To determine how accurate the general assumption transcription start sites to produce multiple RNA transcripts that HSP gene expression is increased in febrile situations is, and use alternative splicing of a transcript to produce multiple the RNA levels of the HSF1 (heat shock transcription factor 1) mature RNAs, as important mechanisms for responding to an gene and certain HSP genes were determined in three cell increased ambient temperature in vitro. lines cultured at 37˚C or 39˚C for three days.
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The HSP70 Chaperone Machinery: J Proteins As Drivers of Functional Specificity
REVIEWS The HSP70 chaperone machinery: J proteins as drivers of functional specificity Harm H. Kampinga* and Elizabeth A. Craig‡ Abstract | Heat shock 70 kDa proteins (HSP70s) are ubiquitous molecular chaperones that function in a myriad of biological processes, modulating polypeptide folding, degradation and translocation across membranes, and protein–protein interactions. This multitude of roles is not easily reconciled with the universality of the activity of HSP70s in ATP-dependent client protein-binding and release cycles. Much of the functional diversity of the HSP70s is driven by a diverse class of cofactors: J proteins. Often, multiple J proteins function with a single HSP70. Some target HSP70 activity to clients at precise locations in cells and others bind client proteins directly, thereby delivering specific clients to HSP70 and directly determining their fate. In their native cellular environment, polypeptides are participates in such diverse cellular functions. Their constantly at risk of attaining conformations that pre- functional diversity is remarkable considering that vent them from functioning properly and/or cause them within and across species, HSP70s have high sequence to aggregate into large, potentially cytotoxic complexes. identity. They share a single biochemical activity: an Molecular chaperones guide the conformation of proteins ATP-dependent client-binding and release cycle com- throughout their lifetime, preventing their aggregation bined with client protein recognition, which is typi- by protecting interactive surfaces against non-productive cally rather promiscuous. This apparent conundrum interactions. Through such inter actions, molecular chap- is resolved by the fact that HSP70s do not work alone, erones aid in the folding of nascent proteins as they are but rather as ‘HSP70 machines’, collaborating with synthesized by ribosomes, drive protein transport across and being regulated by several cofactors.
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Inhibition of the Heat Shock Protein a (HSPA) Family Potentiates the Anticancer Effects of Manumycin A
cells Article Inhibition of the Heat Shock Protein A (HSPA) Family Potentiates the Anticancer Effects of Manumycin A Damian Robert Sojka 1, Sylwia Hasterok 1, Natalia Vydra 1, Agnieszka Toma-Jonik 1, Anna Wieczorek 2 , Agnieszka Gogler-Pigłowska 1 and Dorota Scieglinska 1,* 1 Center for Translational Research and Molecular Biology of Cancer, Maria Sklodowska-Curie National Research Institute of Oncology Gliwice Branch, 44-102 Gliwice, Poland; [email protected] (D.R.S.); [email protected] (S.H.); [email protected] (N.V.); [email protected] (A.T.-J.); [email protected] (A.G.-P.) 2 Division of Medical Biology, Institute of Biology, Jan Kochanowski University, 25-406 Kielce, Poland; [email protected] * Correspondence: [email protected] Abstract: Manumycin A (MA) is a well-tolerated natural antibiotic showing pleiotropic anticancer effects in various preclinical in vitro and in vivo models. Anticancer drugs may themselves act as stressors to induce the cellular adaptive mechanism that can minimize their cytotoxicity. Heat shock proteins (HSPs) as cytoprotective factors can counteract the deleterious effects of various stressful stimuli. In this study, we examined whether the anticancer effects of MA can be counteracted by the mechanism related to HSPs belonging to the HSPA (HSP70) family. We found that MA caused cell type-speciﬁc alterations in the levels of HSPAs. These changes included concomitant upregulation of the stress-inducible (HSPA1 and HSPA6) and downregulation of the non-stress-inducible (HSPA2) Citation: Sojka, D.R.; Hasterok, S.; paralogs. However, neither HSPA1 nor HSPA2 were necessary to provide protection against MA in Vydra, N.; Toma-Jonik, A.; Wieczorek, lung cancer cells.
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Supplementary Material Contents
Supplementary Material Contents Immune modulating proteins identified from exosomal samples.....................................................................2 Figure S1: Overlap between exosomal and soluble proteomes.................................................................................... 4 Bacterial strains:..............................................................................................................................................4 Figure S2: Variability between subjects of effects of exosomes on BL21-lux growth.................................................... 5 Figure S3: Early effects of exosomes on growth of BL21 E. coli .................................................................................... 5 Figure S4: Exosomal Lysis............................................................................................................................................ 6 Figure S5: Effect of pH on exosomal action.................................................................................................................. 7 Figure S6: Effect of exosomes on growth of UPEC (pH = 6.5) suspended in exosome-depleted urine supernatant ....... 8 Effective exosomal concentration....................................................................................................................8 Figure S7: Sample constitution for luminometry experiments..................................................................................... 8 Figure S8: Determining effective concentration .........................................................................................................
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Senescence Inhibits the Chaperone Response to Thermal Stress
SUPPLEMENTAL INFORMATION Senescence inhibits the chaperone response to thermal stress Jack Llewellyn1, 2, Venkatesh Mallikarjun1, 2, 3, Ellen Appleton1, 2, Maria Osipova1, 2, Hamish TJ Gilbert1, 2, Stephen M Richardson2, Simon J Hubbard4, 5 and Joe Swift1, 2, 5 (1) Wellcome Centre for Cell-Matrix Research, Oxford Road, Manchester, M13 9PT, UK. (2) Division of Cell Matrix Biology and Regenerative Medicine, School of Biological Sciences, Faculty of Biology, Medicine and Health, Manchester Academic Health Science Centre, University of Manchester, Manchester, M13 9PL, UK. (3) Current address: Department of Biomedical Engineering, University of Virginia, Box 800759, Health System, Charlottesville, VA, 22903, USA. (4) Division of Evolution and Genomic Sciences, School of Biological Sciences, Faculty of Biology, Medicine and Health, Manchester Academic Health Science Centre, University of Manchester, Manchester, M13 9PL, UK. (5) Correspondence to SJH ([email protected]) or JS ([email protected]). Page 1 of 11 Supplemental Information: Llewellyn et al. Chaperone stress response in senescence CONTENTS Supplemental figures S1 – S5 … … … … … … … … 3 Supplemental table S6 … … … … … … … … 10 Supplemental references … … … … … … … … 11 Page 2 of 11 Supplemental Information: Llewellyn et al. Chaperone stress response in senescence SUPPLEMENTAL FIGURES Figure S1. A EP (passage 3) LP (passage 16) 200 µm 200 µm 1.5 3 B Mass spectrometry proteomics (n = 4) C mRNA (n = 4) D 100k EP 1.0 2 p < 0.0001 p < 0.0001 LP p < 0.0001 p < 0.0001 ) 0.5 1 2 p < 0.0001 p < 0.0001 10k 0.0 0 -0.5 -1 Cell area (µm Cell area fold change vs. EP fold change vs.
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Functional Genomics Study of Acute Heat Stress Response in the Small
www.nature.com/scientificreports OPEN Functional genomics study of acute heat stress response in the small yellow follicles of layer-type Received: 30 January 2017 Accepted: 11 December 2017 chickens Published: xx xx xxxx Chuen-Yu Cheng1, Wei-Lin Tu1, Chao-Jung Chen2,3, Hong-Lin Chan4,5, Chih-Feng Chen1,6,7, Hsin-Hsin Chen1, Pin-Chi Tang1,2, Yen-Pai Lee1, Shuen-Ei Chen1,6,7 & San-Yuan Huang 1,6,7,8 This study investigated global gene and protein expression in the small yellow follicle (SYF; 6–8 mm in diameter) tissues of chickens in response to acute heat stress. Twelve 30-week-old layer-type hens were divided into four groups: control hens were maintained at 25 °C while treatment hens were subjected to acute heat stress at 36 °C for 4 h without recovery, with 2-h recovery, and with 6-h recovery. SYFs were collected at each time point for mRNA and protein analyses. A total of 176 genes and 93 distinct proteins with diferential expressions were identifed, mainly associated with the molecular functions of catalytic activity and binding. The upregulated expression of heat shock proteins and peroxiredoxin family after acute heat stress is suggestive of responsive machineries to protect cells from apoptosis and oxidative insults. In conclusion, both the transcripts and proteins associated with apoptosis, stress response, and antioxidative defense were upregulated in the SYFs of layer-type hens to alleviate the detrimental efects by acute heat stress. However, the genomic regulations of specifc cell type in response to acute heat stress of SYFs require further investigation.
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Cytoplasmic Sequestration of the Tumor Suppressor P53 by a Heat Shock Protein 70 Family Member, Mortalin, in Human Colorectal Adenocarcinoma Cell Lines Erin E
West Chester University Digital Commons @ West Chester University Biology Faculty Publications Biology 2012 Cytoplasmic sequestration of the tumor suppressor p53 by a heat shock protein 70 family member, mortalin, in human colorectal adenocarcinoma cell lines Erin E. Gestl West Chester University of Pennsylvania, [email protected] S. Anne Boettger West Chester University of Pennsylvania, [email protected] Follow this and additional works at: http://digitalcommons.wcupa.edu/bio_facpub Part of the Cancer Biology Commons Recommended Citation Gestl, E. E., & Boettger, S. A. (2012). Cytoplasmic sequestration of the tumor suppressor p53 by a heat shock protein 70 family member, mortalin, in human colorectal adenocarcinoma cell lines. Biochemical and Biophysical Research Communications, 423(2), 411-416. http://dx.doi.org/http://dx.doi.org/10.1016/j.bbrc.2012.05.139 This Article is brought to you for free and open access by the Biology at Digital Commons @ West Chester University. It has been accepted for inclusion in Biology Faculty Publications by an authorized administrator of Digital Commons @ West Chester University. For more information, please contact [email protected]. Biochemical and Biophysical Research Communications xxx (2012) xxx–xxx Contents lists available at SciVerse ScienceDirect Biochemical and Biophysical Research Communications journal homepage: www.elsevier.com/locate/ybbrc Cytoplasmic sequestration of the tumor suppressor p53 by a heat shock protein 70 family member, mortalin, in human colorectal adenocarcinoma cell lines ⇑ Erin E. Gestl 1, S. Anne Böttger Department of Biology, West Chester University, 750 S Church Street, West Chester, PA 19383, USA article info abstract Article history: While it is known that cytoplasmic retention of p53 occurs in many solid tumors, the mechanisms Received 25 May 2012 responsible for this retention have not been positively identiﬁed.
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