VIRUS

1. Parasit kecil yang tidak bisa berbiak secara

mandiri
2. Tergolong materi genetik yang dapat
berpindah (moblile genetic element)
3. Genom berupa DNA atau RNA
4. Umumnya memiliki selaput berupa protein
(capsid) dan atau membran
BENTUK (GEOMETRI) VIRUS
Bentuk dan Ukuran (1)
Bentuk dan Ukuran (2)
 Kapsid

Susunan teratur dari satu atau beberapa jenis

protein (capsomer)
Masing-masing protein disandi oleh gen virus
Membungkus materi genetik virus
Kapsid ditambah materi genetik yang dibungkus,
disebut nukleokapsid
Keunggulan Protein Identik sebagai
Pembentuk Struktur Virus

1.Menghemat Informasi Genetik

2.Mendorong perakitan secara

otomatis (self-assembly)
Viral assembly
Selubung Virus (Viral Envelope)
Contoh Virus Berselubung
Materi Menyerupai Virus
(Atypical Viruslike Agent)

1. Defective Viruses

2. Pseudovirions

3. Viroids

4. Prions
Comparison of Prions and Conventional Viruses

Feature Prions Conventional

Viruses

Particle contains No Yes

nucleic acid
Particle contains Yes, encoded by Yes, encoded by viral
protein cellular genes genes
Inactivated rapidly by No Yes
UV light or heat
Appearance in Filamentous rod Icosahedral or helical
electron microscope (amyloid-like) symetry
Infection induces No Yes
antibody
Infection induces No Yes
inflammation
TIPE GENOM VIRUS
 Complementarity in Viral Genome Replication
Prototype Virus Parental Intermediate Progeny
Genome Form Genome
Poliovirus +ssRNA -ssRNA +ssRNA

Influenza virus, -ssRNA +ssRNA -ssRNA

measles virus,
rabies virus
Rotavirus dsRNA +ssRNA dsRNA

Retrovirus +ssRNA dsDNA ssRNA

Parvovirus B19 ssDNA dsDNA ssDNA

Hepatitis B virus dsDNA +ssRNA dsDNA

Papovavirus, dsDNA dsDNA dsDNA

adenovirus,
herpesvirus,
poxvirus
Penggolongan Virus
 FUNGSI GENOM VIRUS
Menyandi enzim untuk replikasi virus
Menyandi protein capsid

Virus kecil bergantung pada genom inang

untuk replikasi DNA (SV40)
PERAKITAN SELUBUNG VIRUS
 Replikasi Virus

Viral Growth Curve

Viral Growth Cycle (adenovirus)
Siklus Hidup Virus (disederhanakan)
SIKLUS HIDUP SEMLIKI FOREST
VIRUS
SIKLUS HIDUP BACTERIOPHAGE
LAMBDA
RETROVIRUS
PLAQUE ASSAY
Influenza Virus
Enveloped RNA Virus, 80-120 nm

Consists of 8 separate segments:

PB2 (Polymerase B2 protein)
PB1 (Polymerase B1 protein)
PA (Polymerase A protein)
HA or H (Haemagglutinin) :
- Attachment to host cell
NP (Nucleocapsid protein)
NA or N (Neuraminidase) :
- Assist the release of new
virus
M (Matrix protein)
Non-structural protein (NS)
 Adaptation of avian virus to efficient infection of- and
transmission between humans likely involves multiple genes

HA NA

polymerase
(PA, PB1, PB2)
Oseltamivir Resistant-H5N1
Neuraminidase Action
 Summary

Amino acid substitution in neuraminidase (H274Y)

confers high-level resistance to oseltamivir
All patients infected died
Resistance emerged during treatment with oseltamivir
Suggestion: treatment of H5N1 infection should include
additional antiviral agents
 Clinical data
Oseltamivir dose: 75 mg (2X a day, except day 1 : 3X)
Temperature: 40.30C
Pulse: 106 beats/min
Respiratory rate: 36 breath/min
Blood pressure: normal
Serial chest radiograph (day 1,2,3,4,6)
Sequence analysis of neuraminidase gene

T substitution at nucleotide 763 changing codon CAC for 274H to TAC for 274Y

Raw sequencing traces revealed the presence of a minor

subpopulation of wildtype 274 H among predominating 274Y
H5N1 Viral RNA Load from 8 patients
The neuraminidase active site changes shape to create a pocket for oseltamivir, whereas it accommodates zanamivir
without such a change (Panel A). Any of several mutations may prevent the binding of oseltamivir by preventing
the formation of this pocket (Panel B); the oseltamivir-resistant virus can nonetheless bind to the host-cell sialic
acid receptor and to zanamivir. The pocket for oseltamivir, illustrated by key amino acids in Panel C, is created by
the rotation of E276 and bonding of the amino acid to R224 events that are prevented by the mutations R292K,
N294S, and H274Y and therefore result in resistance to oseltamivir. An E119V mutation may permit the binding of
a water molecule in the space created by the smaller valine, also interfering with oseltamivir binding. None of
these mutations prevent the binding of zanamivir or of the natural sialic acid substrate. An animated version of this
figure is available with the full text of the article at www.nejm.org.