Cicatricial alopecia - a case report with a review of literature

Cicatricial alopecia encompasses a group of clinical entities that affect the hair unit leaving permanent destruction of the follicular ostia, skin atrophy and irreversible loss of hair follicles. Herein, a 43-year-old lady with erythematous follicular papules, resulting into atrophic scars with permanent loss of hairs, slowly progressing for more than 22 years, is presented. The patient has been consulted by numerous dermatologists and no exact histological diagnosis was verified. Upon proper clinico-pathological work-up, a diagnosis of lichen planopilaris was concluded and treatment with intralesionaly corticosteroids and oral hydroxychloroquine was introduced. The patient improved significantly during the 3-month follow-up. Scarring alopecia should always be evaluated clinically and by scalp biopsy to accurately analyze the change in the follicular architecture and type, distribution and extent of the inflammatory infiltrate. This complex diagnostic approach is crucial for the diagnosis and management of all cases of cicatricial alopecias

Privatización de los bancos en Corea del Sur

Temas Varios del Pacífico

Crystal Structure of the Hendra Virus Attachment G Glycoprotein Bound to a Potent Cross-Reactive Neutralizing Human Monoclonal Antibody

<div><p>The henipaviruses, represented by Hendra (HeV) and Nipah (NiV) viruses are highly pathogenic zoonotic paramyxoviruses with uniquely broad host tropisms responsible for repeated outbreaks in Australia, Southeast Asia, India and Bangladesh. The high morbidity and mortality rates associated with infection and lack of licensed antiviral therapies make the henipaviruses a potential biological threat to humans and livestock. Henipavirus entry is initiated by the attachment of the G envelope glycoprotein to host cell membrane receptors. Previously, henipavirus-neutralizing human monoclonal antibodies (hmAb) have been isolated using the HeV-G glycoprotein and a human naïve antibody library. One cross-reactive and receptor-blocking hmAb (m102.4) was recently demonstrated to be an effective post-exposure therapy in two animal models of NiV and HeV infection, has been used in several people on a compassionate use basis, and is currently in development for use in humans. Here, we report the crystal structure of the complex of HeV-G with m102.3, an m102.4 derivative, and describe NiV and HeV escape mutants. This structure provides detailed insight into the mechanism of HeV and NiV neutralization by m102.4, and serves as a blueprint for further optimization of m102.4 as a therapeutic agent and for the development of entry inhibitors and vaccines.</p></div

Structure of the m102.3/HeV-G complex, and comparison to the ephrin-B2/HeV-G structure.

<p>A. Left: Overall Structure of the m102.3/HeV-G complex viewed from the side. CDR-H3 (magenta) of m102.3 inserts into the central cavity of HeV-G (green). Disulfide bonds are shown as yellow sticks. The five glycosylation sites of HeV-G are shown as grey spheres. Right: A close up view of the HeVG/m102.3 complex interface. Residues involved in the interaction are shown as stick figures and labeled. The solvent accessible surface of HeV-G central cavity region, viewed from top, is presented on the bottom. CDR-H3 residues (magenta) and R30 (cyan, on the light chain of Fab) and their contacting residues on HeV-G (green) are shown and labeled. B. Overall structure of the ephrin-B2 (orange)/HeV-G (blue) complex. HeV-G in the complex is in the same orientation as in panel A.</p

Comparison of the binding interfaces in the HeV-G/m102.3 and the HeV-G/ephrin-B2 complexes.

<p>A: The solvent accessible surface of the HeV-G molecule in the HeV-G/m102.3 complex viewed from the top. HeV-G is colored in green, except for the m102.3-contacting region that is colored in red (for the 1∶1 complex interface) and in blue (for the region contacted by another copy of the light chain in the hetero-tetrameric 2∶2 complex interface). B: The solvent accessible surface view of the HeV-G molecule in the HeV-G/ephrin-B2 complex viewed from the top. HeV-G is colored in grey, except for the ephrin-B2 contacting region, which is colored in red. C: The tip of the m102.3 CDR-H3 region (in magenta) bound in the HeV-G surface cavity (in green). D: The tip of the ephrin-B2 G-H loop (in yellow) bound in the HeV-G surface cavity (in grey).</p