Blood, Dumbbells
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Pelger–Huët anomaly, congenital and acquired, also pince-nez, laminopathy and a little ebola

BONE MARROW: THERAPY-RELATED MYELODYSPLASTIC SYNDROME Blood smear from an adult female with a myelodysplastic syndrome related to radiotherapy and chemotherapy for Hodgkin disease. A hypogranular neutrophil with a pseudo-Pelger-Huet nucleus is shown. The red blood cells show marked poikilocytosis, in part related to post-splenectomy status. (Wright-Giemsa stain)

Pelger–Huët anomaly is a blood laminopathy associated with the lamin B receptor, wherein several types of white blood cells (neutrophils and eosinophils) have nuclei with unusual shape (being bilobed, peanut or dumbbell-shaped instead of the normal trilobed shape) and unusual structure (coarse and lumpy). It is a genetic disorder with an autosomal dominant inheritance pattern. Heterozygotes are clinically normal, although their neutrophils may be mistaken for immature cells which may cause mistreatment in a clinical setting. Homozygotes tend to have neutrophils with rounded nuclei that do have some functional problems.[citation needed]

  • Hoffmann, Katrin; Dreger, Christine K.; Olins, Ada L.; Olins, Donald E.; Shultz, Leonard D.; Lucke, Barbara; Karl, Hartmut; Kaps, Reinhard; Müller, Dietmar; Vayá, Amparo; Aznar, Justo; Ware, Russell E.; Cruz, Norberto Sotelo; Lindner, Tom H.; Herrmann, Harald; Reis, André; Sperling, Karl (2002). “Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger–Huët anomaly)”. Nature Genetics. 31 (4): 410–4. doi:10.1038/ng925. PMID 12118250. S2CID 6020153.
  • “Pelger-Huet anomaly”. Disease Infosearch. Retrieved 2020-04-27. Creative Commons Attribution 3.0 License

Laminopathies are a group of rare genetic disorders caused by mutations in genes encoding proteins of the nuclear lamina. They are included in the more generic term nuclear envelopathies that was coined in 2000 for diseases associated with defects of the nuclear envelope. Since the first reports of laminopathies in the late 1990s, increased research efforts have started to uncover the vital role of nuclear envelope proteins in cell and tissue integrity in animals.

Laminopathies and other nuclear envelopathies have a large variety of clinical symptoms including skeletal and/or cardiac muscular dystrophy, lipodystrophy and diabetes, dysplasia, dermo- or neuropathy, leukodystrophy, and progeria (premature aging). Most of these symptoms develop after birth, typically during childhood or adolescence. Some laminopathies however may lead to an early death, and mutations of lamin B1 (LMNB1 gene) may be lethal before or at birth. Patients with classical laminopathy have mutations in the gene coding for lamin A/C (LMNA gene).[citation needed]

Mutations in the gene coding for lamin B2 (LMNB2 gene) have been linked to Barraquer-Simons syndrome and duplication in the gene coding for lamin B1 (LMNB1 gene) cause autosomal dominant leukodystrophy. Mutations implicated in other nuclear envelopathies were found in genes coding for lamin-binding proteins such as lamin B receptor (LBR gene), emerin (EMD gene) and LEM domain-containing protein 3 (LEMD3 gene) and prelamin A-processing enzymes such as the zinc metalloproteinase STE24 (ZMPSTE24 gene). Mutations causing laminopathies include recessive as well as dominant alleles with rare de novo mutations creating dominant alleles that do not allow their carriers to reproduce before death.[citation needed] The nuclear envelopathy with the highest frequency in human populations is Emery–Dreifuss muscular dystrophy caused by an X-linked mutation in the EMD gene coding for emerin and affecting an estimated 1 in 100,000 people.[citation needed]

Types of known laminopathies and other nuclear envelopathies

SyndromeOMIM IDSymptomsMutation inIdentified in
Atypical Werner syndrome277700Progeria with increased severity compared to normal Werner syndromeLamin A/C2003
Barraquer–Simons syndrome608709LipodystrophyLamin B22006
Buschke–Ollendorff syndrome166700Skeletal dysplasia, skin lesionsLEM domain containing protein 3 (lamin-binding protein)2004
Cardiomyopathy, dilated, with quadriceps myopathy607920CardiomyopathyLamin A/C2003[
Charcot–Marie–Tooth disease, axonal, type 2B1605588NeuropathyLamin A/C2002
Emery–Dreifuss muscular dystrophy, X-linked (EDMD)310300Skeletal and cardiac muscular dystrophyEmerin (lamin-binding protein)1996, 2000
Emery–Dreifuss muscular dystrophy, autosomal dominant (EDMD2)181350Skeletal and cardiac muscular dystrophyLamin A/C1999
Emery–Dreifuss muscular dystrophy, autosomal recessive (EDMD3)604929Skeletal and cardiac muscular dystrophyLamin A/C2000
Familial partial lipodystrophy of the Dunnigan type (FPLD)151660Lipoatrophic diabetesLamin A/C2002
Greenberg dysplasia215140Skeletal dysplasiaLamin B receptor2003
Hutchinson–Gilford progeria syndrome (HGPS)176670ProgeriaLamin A/C2003
Leukodystrophy, demyelinating, adult-onset, autosomal dominant (ADLD)169500Progressive demyelinating disorder affecting the central nervous systemLamin B1 (tandem gene duplication)2006
Limb-girdle muscular dystrophy type 1B (LGMD1B)159001Muscular dystrophy of hips and shoulders, cardiomyopathyLamin A/C2000
Lipoatrophy with diabetes, hepatic steatosis, hypertrophic cardiomyopathy, and leukomelanodermic papules (LDHCP)608056Lipoatrophic diabetes, fatty liver, hypertrophic cardiomyopathy, skin lesionsLamin A/C2003
Mandibuloacral dysplasia with type A lipodystrophy (MADA)248370Dysplasia and lipodystrophyLamin A/C2002
Mandibuloacral dysplasia with type B lipodystrophy (MADB)608612Dysplasia and lipodystrophyZinc metalloprotease STE24 (prelamin-processing enzyme)2003
Pelger–Huet anomaly (PHA)169400MyelodysplasiaLamin B receptor2002
Restrictive dermopathy, lethal275210DermopathyLamin A/C or Zinc metalloprotease STE24 (prelamin-processing enzyme)2004

Currently, there is no cure for laminopathies and treatment is largely symptomatic and supportive. Physical therapy and/or corrective orthopedic surgery may be helpful for patients with muscular dystrophies. Laminopathies affecting heart muscle may cause heart failure requiring treatment with medications including ACE inhibitors, beta blockers and aldosterone antagonists, while the abnormal heart rhythms that frequently occur in these patients may require a pacemaker or implantable defibrillator. Treatment for neuropathies may include medication for seizures and spasticity.[citation needed]

The recent progress in uncovering the molecular mechanisms of toxic progerin formation in laminopathies leading to premature aging has opened up the potential for the development of targeted treatment. The farnesylation of prelamin A and its pathological form progerin is carried out by the enzyme farnesyl transferase. Farnesyl transferase inhibitors (FTIs) can be used effectively to reduce symptoms in two mouse model systems for progeria and to revert the abnormal nuclear morphology in progeroid cell cultures. Two oral FTIs, lonafarnib and tipifarnib, are already in use as anti-tumor medication in humans and may become avenues of treatment for children with laminopathic progeria. Nitrogen-containing bisphosphate drugs used in the treatment of osteoporosis reduce farnesyldiphosphate production and thus prelamin A farnesylation. Testing of these drugs may prove them to be useful in treating progeria as well. The use of antisense oligonucleotides to inhibit progerin synthesis in affected cells is another avenue of current research into the development of anti-progerin drugs.

Congenital Pelger–Huët anomaly

Is a benign dominantly inherited defect of terminal neutrophil differentiation as a result of mutations in the lamin B receptor gene. The characteristic leukocyte appearance was first reported in 1928 by Karel Pelger (1885-1931), a Dutch Hematologist, who described leukocytes with dumbbell-shaped bilobed nuclei, a reduced number of nuclear segments, and coarse clumping of the nuclear chromatin. In 1931, Gauthier Jean Huet (1879-1970), a Dutch Pediatrician, identified it as an inherited disorder.

It is a genetic disorder with an autosomal dominant inheritance pattern. Heterozygotes are clinically normal, although their neutrophils may be mistaken for immature cells, which may cause mistreatment in a clinical setting. Homozygotes tend to have neutrophils with rounded nuclei that do have some functional problems. Homozygous individuals inconsistently have skeletal anomalies such as post-axial polydactyly, short metacarpals, short upper limbs, short stature, or hyperkyphosis.[citation needed]

  • Hoffmann, Katrin; Dreger, Christine K.; Olins, Ada L.; Olins, Donald E.; Shultz, Leonard D.; Lucke, Barbara; Karl, Hartmut; Kaps, Reinhard; Müller, Dietmar; Vayá, Amparo; Aznar, Justo; Ware, Russell E.; Cruz, Norberto Sotelo; Lindner, Tom H.; Herrmann, Harald; Reis, André; Sperling, Karl (2002). “Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger–Huët anomaly)”. Nature Genetics. 31 (4): 410–4. doi:10.1038/ng925. PMID 12118250. S2CID 6020153.
  • Vale, A. M.; Tomaz, L. R.; Sousa, R. S.; Soto-Blanco, B. (2011). “Pelger-Huët anomaly in two related mixed-breed dogs”. Journal of Veterinary Diagnostic Investigation. 23 (4): 863–5. doi:10.1177/1040638711407891. PMID 21908340.

Identifying Pelger–Huët anomaly is important to differentiate from bandemia with a left-shifted peripheral blood smear and neutrophilic band forms and from an increase in young neutrophilic forms that can be observed in association with infection.[citation needed]

Acquired or pseudo-Pelger–Huët anomaly

Anomalies resembling Pelger–Huët anomaly that are acquired rather than congenital have been described as pseudo Pelger–Huët anomaly. These can develop in the course of acute myelogenous leukemia or chronic myelogenous leukemia and in myelodysplastic syndrome. It has also been described in Filovirus disease.

In patients with these conditions, the pseudo–Pelger–Huët cells tend to appear late in the disease and often appear after considerable chemotherapy has been administered. The morphologic changes have also been described in myxedema associated with panhypopituitarism, vitamin B12 and folate deficiency, multiple myeloma, enteroviral infections, malaria, muscular dystrophy, leukemoid reaction secondary to metastases to the bone marrow, and drug sensitivity, sulfa and valproate toxicities are examples. In some of these conditions, especially the drug-induced cases, it is important to differentiate between Pelger–Huët anomaly and pseudo-Pelger–Huët to prevent the need for further unnecessary testing for cancer.[citation needed]

Peripheral blood smear shows a predominance of neutrophils with bilobed nuclei which are composed of two nuclear masses connected with a thin filament of chromatin. It resembles the pince-nez glasses, so it is often referred to as pince-nez appearance. Usually the congenital form is not associated with thrombocytopenia and leukopenia, so if these features are present more detailed search for myelodysplasia is warranted, as pseudo-Pelger–Huët anomaly can be an early feature of myelodysplasia.

Filoviridae is a family of single-stranded negative-sense RNA viruses in the order Mononegavirales. Two members of the family that are commonly known are Ebola virus and Marburg virus. Both viruses, and some of their lesser known relatives, cause severe disease in humans and nonhuman primates in the form of viral hemorrhagic fevers.

All filoviruses are classified by the US as select agents, by the World Health Organization as Risk Group 4 Pathogens (requiring Biosafety Level 4-equivalent containment), by the National Institutes of Health/National Institute of Allergy and Infectious Diseases as Category A Priority Pathogens, and by the Centers for Disease Control and Prevention as Category A Bioterrorism Agents, and are listed as Biological Agents for Export Control by the Australia Group.

The family Filoviridae is a virological taxon that was defined in 1982 and emended in 1991, 1998,[10] 2000, 2005, 2010 and 2011. The family currently includes the six virus genera Cuevavirus, Dianlovirus, Ebolavirus, Marburgvirus, Striavirus, and Thamnovirus and is included in the order Mononegavirales. The members of the family (i.e. the actual physical entities) are called filoviruses or filovirids. The name Filoviridae is derived from the Latin noun filum (alluding to the filamentous morphology of filovirions) and the taxonomic suffix -viridae (which denotes a virus family). According to the rules for taxon naming established by the International Committee on Taxonomy of Viruses (ICTV), the name Filoviridae is always to be capitalized, italicized, never abbreviated, and to be preceded by the word “family”. The names of its members (filoviruses or filovirids) are to be written in lower case, are not italicized, and used without articles.

  • Kiley MP, Bowen ET, Eddy GA, Isaäcson M, Johnson KM, McCormick JB, Murphy FA, Pattyn SR, Peters D, Prozesky OW, Regnery RL, Simpson DI, Slenczka W, Sureau P, van der Groen G, Webb PA, Wulff H (1982). “Filoviridae: A taxonomic home for Marburg and Ebola viruses?”. Intervirology. 18 (1–2): 24–32. doi:10.1159/000149300. PMID 7118520.
  • McCormick, J. B. (1991). “Family Filoviridae”. In Francki, R. I. B.; Fauquet, C. M.; Knudson, D. L.; et al. (eds.). Classification and Nomenclature of Viruses-Fifth Report of the International Committee on Taxonomy of Viruses. Archives of Virology Supplement. Vol. 2. Vienna, Austria: Springer. pp. 247–49. ISBN 0-387-82286-0.
  • Jahrling, P. B.; Kiley, M. P.; Klenk, H.-D.; Peters, C. J.; Sanchez, A.; Swanepoel, R. (1995). “Family Filoviridae”. In Murphy, F. A.; Fauquet, C. M.; Bishop, D. H. L.; Ghabrial, S. A.; Jarvis, A. W.; Martelli, G. P.; Mayo, M. A.; Summers, M. D. (eds.). Virus Taxonomy—Sixth Report of the International Committee on Taxonomy of Viruses. Archives of Virology Supplement. Vol. 10. Vienna, Austria: Springer. pp. 289–92. ISBN 3-211-82594-0.
  • Netesov, S.V.; Feldmann, H.; Jahrling, P. B.; Klenk, H. D.; Sanchez, A. (2000). “Family Filoviridae”. In van Regenmortel, M. H. V.; Fauquet, C. M.; Bishop, D. H. L.; Carstens, E. B.; Estes, M. K.; Lemon, S. M.; Maniloff, J.; Mayo, M. A.; McGeoch, D. J.; Pringle, C. R.; Wickner, R. B. (eds.). Virus Taxonomy—Seventh Report of the International Committee on Taxonomy of Viruses. San Diego, USA: Academic Press. pp. 539–48. ISBN 0-12-370200-3.
  • Feldmann, H.; Geisbert, T. W.; Jahrling, P. B.; Klenk, H.-D.; Netesov, S. V.; Peters, C. J.; Sanchez, A.; Swanepoel, R.; Volchkov, V. E. (2005). “Family Filoviridae”. In Fauquet, C. M.; Mayo, M. A.; Maniloff, J.; Desselberger, U.; Ball, L. A. (eds.). Virus Taxonomy—Eighth Report of the International Committee on Taxonomy of Viruses. San Diego, USA: Elsevier/Academic Press. pp. 645–653. ISBN 0-12-370200-3.
  • Kuhn JH, Becker S, Ebihara H, Geisbert TW, Johnson KM, Kawaoka Y, Lipkin WI, Negredo AI, Netesov SV, Nichol ST, Palacios G, Peters CJ, Tenorio A, Volchkov VE, Jahrling PB (2010). “Proposal for a revised taxonomy of the family Filoviridae: Classification, names of taxa and viruses, and virus abbreviations”. Archives of Virology. 155 (12): 2083–2103. doi:10.1007/s00705-010-0814-x. PMC 3074192. PMID 21046175.
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Replication cycle of filoviruses and vectors
Replication cycle of filoviruses at and inside host cell

The filovirus life cycle begins with virion attachment to specific cell-surface receptors, followed by fusion of the virion envelope with cellular membranes and the concomitant release of the virus nucleocapsid into the cytosol. The viral RNA-dependent RNA polymerase (RdRp, or RNA replicase) partially uncoats the nucleocapsid and transcribes the genes into positive-stranded mRNAs, which are then translated into structural and nonstructural proteins. Filovirus RdRps bind to a single promoter located at the 3′ end of the genome. Transcription either terminates after a gene or continues to the next gene downstream. This means that genes close to the 3′ end of the genome are transcribed in the greatest abundance, whereas those toward the 5′ end are least likely to be transcribed. The gene order is therefore a simple but effective form of transcriptional regulation. The most abundant protein produced is the nucleoprotein, whose concentration in the cell determines when the RdRp switches from gene transcription to genome replication. Replication results in full-length, positive-stranded antigenomes that are in turn transcribed into negative-stranded virus progeny genome copies. Newly synthesized structural proteins and genomes self-assemble and accumulate near the inside of the cell membrane. Virions bud off from the cell, gaining their envelopes from the cellular membrane they bud from. The mature progeny particles then infect other cells to repeat the cycle.

  • Feldmann, H.; Geisbert, T. W.; Jahrling, P. B.; Klenk, H.-D.; Netesov, S. V.; Peters, C. J.; Sanchez, A.; Swanepoel, R.; Volchkov, V. E. (2005). “Family Filoviridae”. In Fauquet, C. M.; Mayo, M. A.; Maniloff, J.; Desselberger, U.; Ball, L. A. (eds.). Virus Taxonomy—Eighth Report of the International Committee on Taxonomy of Viruses. San Diego, USA: Elsevier/Academic Press. pp. 645–653. ISBN 0-12-370200-3.

A virus that fulfills the criteria for being a member of the order Mononegavirales is a member of the family Filoviridae if:

Genus nameSpecies nameVirus name (abbreviation)
CuevavirusLloviu cuevavirusLloviu virus (LLOV)
DianlovirusMengla dianlovirusMěnglà virus (MLAV)
EbolavirusBombali ebolavirusBombali virus (BOMV)
Bundibugyo ebolavirusBundibugyo virus (BDBV; previously BEBOV)
Reston ebolavirusReston virus (RESTV; previously REBOV)
Sudan ebolavirusSudan virus (SUDV; previously SEBOV)
Taï Forest ebolavirusTaï Forest virus (TAFV; previously CIEBOV)
Zaire ebolavirusEbola virus (EBOV; previously ZEBOV)
MarburgvirusMarburg marburgvirusMarburg virus (MARV)
Ravn virus (RAVV)
StriavirusXilang striavirusXīlǎng virus (XILV)
ThamnovirusHuangjiao thamnovirusHuángjiāo virus (HUJV)

Filoviruses have a history that dates back several tens of million of years. Endogenous viral elements (EVEs) that appear to be derived from filovirus-like viruses have been identified in the genomes of bats, rodents, shrews, tenrecs, tarsiers, and marsupials. Although most filovirus-like EVEs appear to be pseudogenes, evolutionary analyses suggest that orthologs isolated from several species of the bat genus Myotis have been maintained by selection.

There are presently very limited vaccines for known filovirus. An effective vaccine against EBOV, developed in Canada, was approved for use in 2019 in the US and Europe. Similarly, efforts to develop a vaccine against Marburg virus are under way.

There has been a pressing concern that a very slight genetic mutation to a filovirus such as EBOV could result in a change in transmission system from direct body fluid transmission to airborne transmission, as was seen in Reston virus (another member of genus Ebolavirus) between infected macaques. A similar change in the current circulating strains of EBOV could greatly increase the infection and disease rates caused by EBOV. However, there is no record of any Ebola strain ever having made this transition in humans. The Department of Homeland Security’s National Biodefense Analysis and Countermeasures Center considers the risk of a mutated Ebola virus strain with aerosol transmission capability emerging in the future as a serious threat to national security and has collaborated with the Centers for Disease Control and Prevention (CDC) to design methods to detect EBOV aerosols.

References

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  3. “Pelger-Huet anomaly”. Disease Infosearch. Retrieved 2020-04-27. Creative Commons Attribution 3.0 License
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Further reading

External links

Cytoskeletal defects
Blood film findings
Filoviridae
Zoonotic viral diseases (A80–B34, 042–079)
Taxon identifiersWikidata: Q46305Wikispecies: FiloviridaeCoL: 62448EoL: 5024GBIF: 7759IRMNG: 107125NCBI: 11266WoRMS: 600065

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